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Francis, Monika K.
Alternative names
Publications (10 of 16) Show all publications
Costa, T., Francis, M. K., Farag, S., Edgren, T. & Francis, M. S. (2019). Measurement of Yersinia translocon pore formation in erythrocytes. In: Viveka Vadyvaloo and Matthew B. Lawrenz (Ed.), Pathogenic Yersinia: methods and protocols (pp. 211-229). New York, NY, U.S.A.: Humana Press
Open this publication in new window or tab >>Measurement of Yersinia translocon pore formation in erythrocytes
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2019 (English)In: Pathogenic Yersinia: methods and protocols / [ed] Viveka Vadyvaloo and Matthew B. Lawrenz, New York, NY, U.S.A.: Humana Press, 2019, p. 211-229Chapter in book (Refereed)
Abstract [en]

Many Gram-negative pathogens produce a type III secretion system capable of intoxicating eukaryotic cells with immune-modulating effector proteins. Fundamental to this injection process is the prior secretion of two translocator proteins destined for injectisome translocon pore assembly within the host cell plasma membrane. It is through this pore that effectors are believed to travel to gain access to the host cell interior. Yersinia species especially pathogenic to humans and animals assemble this translocon pore utilizing two hydrophobic translocator proteins-YopB and YopD. Although a full molecular understanding of the biogenesis, function and regulation of this translocon pore and subsequent effector delivery into host cells remains elusive, some of what we know about these processes can be attributed to studies of bacterial infections of erythrocytes. Herein we describe the methodology of erythrocyte infections by Yersinia, and how analysis of the resultant contact-dependent hemolysis can serve as a relative measurement of YopB- and YopD-dependent translocon pore formation.

Place, publisher, year, edition, pages
New York, NY, U.S.A.: Humana Press, 2019
Series
Methods in Molecular Biology, ISSN 1064-3745, E-ISSN 1940-6029 ; 2010
Keywords
Biogenesis, Contact-dependent hemolysis, Effector recognition and intracellular delivery, Function and regulation, Host immune response, Membrane integration, Type III translocon pore complex
National Category
Microbiology in the medical area Microbiology Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Research subject
Microbiology; Molecular Biology; Infectious Diseases
Identifiers
urn:nbn:se:umu:diva-161385 (URN)10.1007/978-1-4939-9541-7_15 (DOI)31177441 (PubMedID)978-1-4939-9540-0 (ISBN)
Funder
Swedish Research Council, 2014-2105Swedish Research Council, 2009-5628
Available from: 2019-07-03 Created: 2019-07-03 Last updated: 2019-07-03Bibliographically approved
Thanikkal, E. J., Kumar Gahlot, D., Liu, J., Fredriksson Sundbom, M., Gurung, J. M., Ruuth, K., . . . Francis, M. S. (2019). The Yersinia pseudotuberculosis Cpx envelope stress system contributes to transcriptional activation of rovM. Virulence, 10(1), 37-57
Open this publication in new window or tab >>The Yersinia pseudotuberculosis Cpx envelope stress system contributes to transcriptional activation of rovM
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2019 (English)In: Virulence, ISSN 2150-5594, E-ISSN 2150-5608, Vol. 10, no 1, p. 37-57Article in journal (Refereed) Published
Abstract [en]

The Gram-negative enteropathogen Yersinia pseudotuberculosis possesses a number of regulatory systems that detect cell envelope damage caused by noxious extracytoplasmic stresses. The CpxA sensor kinase and CpxR response regulator two-component regulatory system is one such pathway. Active Cpx signalling upregulates various factors designed to repair and restore cell envelope integrity. Concomitantly, this pathway also down-regulates key determinants of virulence. In Yersinia, cpxA deletion accumulates high levels of phosphorylated CpxR (CpxR~P). Accumulated CpxR~P directly repressed rovA expression and this limited expression of virulence-associated processes. A second transcriptional regulator, RovM, also negatively regulates rovA expression in response to nutrient stress. Hence, this study aimed to determine if CpxR~P can influence rovA expression through control of RovM levels. We determined that the active CpxR~P isoform bound to the promoter of rovM and directly induced its expression, which naturally associated with a concurrent reduction in rovA expression. Site-directed mutagenesis of the CpxR~P binding sequence in the rovM promoter region desensitised rovM expression to CpxR~P. These data suggest that accumulated CpxR~P inversely manipulates the levels of two global transcriptional regulators, RovA and RovM, and this would be expected to have considerable influence on Yersinia pathophysiology and metabolism.

Place, publisher, year, edition, pages
Taylor & Francis Group, 2019
Keywords
Environmental stress responsiveness, gene expression control, metabolic networks, microbial behaviour, growth and survival, fitness
National Category
Microbiology Microbiology in the medical area
Research subject
Microbiology; Molecular Biology; Infectious Diseases
Identifiers
urn:nbn:se:umu:diva-154425 (URN)10.1080/21505594.2018.1556151 (DOI)000453473300001 ()30518290 (PubMedID)
Funder
Swedish Research Council, 2009-3660Swedish Research Council, 2014-6652
Available from: 2018-12-17 Created: 2018-12-17 Last updated: 2019-03-05Bibliographically approved
Gurung, J. M., Amer, A., Francis, M., Costa, T., Chen, S., Zavialov, A. V. & Francis, M. S. (2018). Heterologous complementation studies with the YscX and YscY protein families reveals a specificity for Yersinia pseudotuberculosis type III secretion. Frontiers in Cellular and Infection Microbiology, 8, Article ID 80.
Open this publication in new window or tab >>Heterologous complementation studies with the YscX and YscY protein families reveals a specificity for Yersinia pseudotuberculosis type III secretion
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2018 (English)In: Frontiers in Cellular and Infection Microbiology, E-ISSN 2235-2988, Vol. 8, article id 80Article in journal (Refereed) Published
Abstract [en]

Type III secretion systems harbored by several Gram-negative bacteria are often used to deliver host-modulating effectors into infected eukaryotic cells. About 20 core proteins are needed for assembly of a secretion apparatus. Several of these proteins are genetically and functionally conserved in type III secretion systems of bacteria associated with invertebrate or vertebrate hosts. In the Ysc family of type III secretion systems are two poorly characterized protein families, the YscX family and the YscY family. In the plasmid-encoded Ysc-Yop type III secretion system of human pathogenic Yersinia species, YscX is a secreted substrate while YscY is its non-secreted cognate chaperone. Critically, neither an yscX nor yscY null mutant of Yersinia is capable of type III secretion. In this study, we show that the genetic equivalents of these proteins produced as components of other type III secretion systems of Pseudomonas aeruginosa (PscX and PscY), Aeromonas species (AscX and AscY), Vibrio species (VscX and VscY), and Photorhabdus luminescens (SctX and SctY) all possess an ability to interact with its native cognate partner and also establish cross-reciprocal binding to non-cognate partners as judged by a yeast two-hybrid assay. Moreover, a yeast three-hybrid assay also revealed that these heterodimeric complexes could maintain an interaction with YscV family members, a core membrane component of all type III secretion systems. Despite maintaining these molecular interactions, only expression of the native yscX in the near full-length yscX deletion and native yscY in the near full-length yscY deletion were able to complement for their general substrate secretion defects. Hence, YscX and YscY must have co-evolved to confer an important function specifically critical for Yersinia type III secretion.

Place, publisher, year, edition, pages
Frontiers Research Foundation, 2018
Keywords
T3S chaperone, secretion hierarchy, substrate sorting, LcrH/SycD, YscV, protein-protein interaction
National Category
Microbiology
Research subject
Microbiology; Molecular Biology; Infectious Diseases
Identifiers
urn:nbn:se:umu:diva-146348 (URN)10.3389/fcimb.2018.00080 (DOI)000427608900001 ()29616194 (PubMedID)
Funder
Swedish Research Council
Available from: 2018-04-05 Created: 2018-04-05 Last updated: 2018-06-09Bibliographically approved
Vdovikova, S., Luhr, M., Szalai, P., Skalman, L. N., Francis, M. K., Lundmark, R., . . . Wai, S. N. (2017). A Novel Role of Listeria monocytogenes Membrane Vesicles in Inhibition of Autophagy and Cell Death. Frontiers in Cellular and Infection Microbiology, 7, Article ID 154.
Open this publication in new window or tab >>A Novel Role of Listeria monocytogenes Membrane Vesicles in Inhibition of Autophagy and Cell Death
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2017 (English)In: Frontiers in Cellular and Infection Microbiology, E-ISSN 2235-2988, Vol. 7, article id 154Article in journal (Refereed) Published
Abstract [en]

Bacterial membrane vesicle (MV) production has been mainly studied in Gram-negative species. In this study, we show that Listeria monocytogenes, a Gram-positive pathogen that causes the food-borne illness listeriosis, produces MVs both in vitro and in vivo. We found that a major virulence factor, the pore-forming hemolysin listeriolysin O (LLO), is tightly associated with the MVs, where it resides in an oxidized, inactive state. Previous studies have shown that LLO may induce cell death and autophagy. To monitor possible effects of LLO and MVs on autophagy, we performed assays for LC3 lipidation and LDH sequestration as well as analysis by confocal microscopy of HEK293 cells expressing GFP-LC3. The results revealed that MVs alone did not affect autophagy whereas they effectively abrogated autophagy induced by pure LLO or by another pore-forming toxin from Vibrio cholerae, VCC. Moreover, Listeria monocytogenes MVs significantly decreased Torin1-stimulated macroautophagy. In addition, MVs protected against necrosis of HEK293 cells caused by the lytic action of LLO. We explored the mechanisms of LLO-induced autophagy and cell death and demonstrated that the protective effect of MVs involves an inhibition of LLO-induced pore formation resulting in inhibition of autophagy and the lytic action on eukaryotic cells. Further, we determined that these MVs help bacteria to survive inside eukaryotic cells (mouse embryonic fibroblasts). Taken together, these findings suggest that intracellular release of MVs from L. monocytogenes may represent a bacterial strategy to survive inside host cells, by its control of LLO activity and by avoidance of destruction from the autophagy system during infection.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2017
Keywords
Listeria monocytogenes, membrane vesicles, autophagy, listeriolysin O, pore-forming toxin
National Category
Immunology in the medical area Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-136187 (URN)10.3389/fcimb.2017.00154 (DOI)000400405800001 ()28516064 (PubMedID)
Available from: 2017-07-07 Created: 2017-07-07 Last updated: 2018-06-09Bibliographically approved
Vidal-Quadras, M., Holst, M. R., Francis, M. K., Larsson, E., Hachimi, M., Yau, W.-L., . . . Lundmark, R. (2017). Endocytic turnover of Rab8 controls cell polarization. Journal of Cell Science, 130(6), 1147-1157
Open this publication in new window or tab >>Endocytic turnover of Rab8 controls cell polarization
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2017 (English)In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 130, no 6, p. 1147-1157Article in journal (Refereed) Published
Abstract [en]

Adaptation of cell shape and polarization through the formation and retraction of cellular protrusions requires balancing of endocytosis and exocytosis combined with fine-tuning of the local activity of small GTPases like Rab8. Here, we show that endocytic turnover of the plasma membrane at protrusions is directly coupled to surface removal and inactivation of Rab8. Removal is induced by reduced membrane tension and mediated by the GTPase regulator associated with focal adhesion kinase-1 (GRAF1, also known as ARHGAP26), a regulator of clathrin-independent endocytosis. GRAF1-depleted cells were deficient in multi-directional spreading and displayed elevated levels of GTP-loaded Rab8, which was accumulated at the tips of static protrusions. Furthermore, GRAF1 depletion impaired lumen formation and spindle orientation in a 3D cell culture system, indicating that GRAF1 activity regulates polarity establishment. Our data suggest that GRAF1-mediated removal of Rab8 from the cell surface restricts its activity during protrusion formation, thereby facilitating dynamic adjustment of the polarity axis.

Keywords
Rab8, GRAF1, Cell polarization, Endocytosis
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:umu:diva-133762 (URN)10.1242/jcs.195420 (DOI)000397907900012 ()28137756 (PubMedID)
Funder
Swedish Research Council, 811-2014-59Swedish Foundation for Strategic Research , FFL09-0181The Kempe Foundations, SMK1348
Available from: 2017-05-03 Created: 2017-05-03 Last updated: 2018-06-09Bibliographically approved
Francis, M. K., Holst, M. R., Vidal-Quadras, M., Henriksson, S., Santarella-Mellwig, R., Sandblad, L. & Lundmark, R. (2015). Endocytic membrane turnover at the leading edge is driven by a transient interaction between Cdc42 and GRAF1. Journal of Cell Science, 128(22), 4183-4195
Open this publication in new window or tab >>Endocytic membrane turnover at the leading edge is driven by a transient interaction between Cdc42 and GRAF1
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2015 (English)In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 128, no 22, p. 4183-4195Article in journal (Refereed) Published
Abstract [en]

Changes in cell morphology require coordination of plasma membrane turnover and cytoskeleton dynamics, processes that are regulated by Rho GTPases. Here, we describe how a direct interaction between the Rho GTPase Cdc42 and the GTPase activating protein (GAP) GRAF1, facilitate rapid cell surface turnover at the leading edge. Both Cdc42 and GRAF1 were required for fluid phase uptake and regulated the generation of transient GRAF1-coated endocytic carriers, distinct from clathrin coated vesicles. GRAF1 was found to transiently assemble at discrete Cdc42-enriched punctae at the plasma membrane resulting in a corresponding decrease in Cdc42 microdomain association. However, Cdc42 captured in its active state was, via a GAP domain mediated interaction, localised together with GRAF1 on accumulated internal structures derived from the cell surface. Correlative fluorescence and electron tomography microscopy revealed that these structures were clusters of small membrane carriers affected in their endosomal processing. We conclude that a transient interaction between Cdc42 and GRAF1 drives endocytic turnover and controls the transition essential for endosomal maturation of plasma membrane internalised by this mechanism.

National Category
Biochemistry and Molecular Biology Cell Biology
Research subject
Medical Biochemistry
Identifiers
urn:nbn:se:umu:diva-111228 (URN)10.1242/jcs.174417 (DOI)000366314900017 ()26446261 (PubMedID)
Available from: 2015-11-11 Created: 2015-11-10 Last updated: 2018-06-07Bibliographically approved
Rompikuntal, P. K., Vdovikova, S., Duperthuy, M., Johnson, T. L., Åhlund, M., Lundmark, R., . . . Wai, S. N. (2015). Outer Membrane Vesicle-Mediated Export of Processed PrtV Protease from Vibrio cholerae. PLoS ONE, 10(7), Article ID e0134098.
Open this publication in new window or tab >>Outer Membrane Vesicle-Mediated Export of Processed PrtV Protease from Vibrio cholerae
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2015 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 10, no 7, article id e0134098Article in journal (Refereed) Published
Abstract [en]

Background Outer membrane vesicles (OMVs) are known to release from almost all Gram-negative bacteria during normal growth. OMVs carry different biologically active toxins and enzymes into the surrounding environment. We suggest that OMVs may therefore be able to transport bacterial proteases into the target host cells. We present here an analysis of the Vibrio cholerae OMV-associated protease PrtV. Methodology/Principal Findings In this study, we demonstrated that PrtV was secreted from the wild type V. cholerae strain C6706 via the type II secretion system in association with OMVs. By immunoblotting and electron microscopic analysis using immunogold labeling, the association of PrtV with OMVs was examined. We demonstrated that OMV-associated PrtV was biologically active by showing altered morphology and detachment of cells when the human ileocecum carcinoma (HCT8) cells were treated with OMVs from the wild type V. cholerae strain C6706 whereas cells treated with OMVs from the prtV isogenic mutant showed no morphological changes. Furthermore, OMV-associated PrtV protease showed a contribution to bacterial resistance towards the antimicrobial peptide LL-37. Conclusion/Significance Our findings suggest that OMVs released from V. cholerae can deliver a processed, biologically active form of PrtV that contributes to bacterial interactions with target host cells.

National Category
Other Basic Medicine
Identifiers
urn:nbn:se:umu:diva-107868 (URN)10.1371/journal.pone.0134098 (DOI)000358836800103 ()26222047 (PubMedID)
Available from: 2015-09-16 Created: 2015-08-28 Last updated: 2018-06-07Bibliographically approved
Francis, M. K. (2015). Regulation of GRAF1 membrane sculpting function during cell movement. (Doctoral dissertation). Umeå: Umeå University
Open this publication in new window or tab >>Regulation of GRAF1 membrane sculpting function during cell movement
2015 (English)Doctoral thesis, comprehensive summary (Other academic)
Alternative title[sv]
Reglering av den membranskulpterande funktionen hos GRAF1 vid cellrörelse
Abstract [en]

All eukaryotic cells rely on endocytic events to satisfy a constant need for nutrient and fluid uptake from their surroundings. Endocytosis-dependent turnover of cell surface constituents also serves to control signal transduction and establish morphological changes in response to extracellular stimuli. During endocytosis, distinct protein machineries re-sculpt the plasma membrane into vesicular carriers that enclose molecules that are to be taken up into the cell. Besides those produced from the canonical clathrin-mediated endocytic machinery, it is becoming increasingly clear that other membrane carriers exist. The indisputable connection between the function of these uptake systems and various disease states, highlights why it is so important to increase our knowledge about the underlying molecular machineries.

The aim of this thesis was therefore to characterise the function of GRAF1, a protein suggested to be a tumour suppressor due to that the gene has been found to be mutated in certain cancer patients. My work focused on understanding how this protein operates during formation of clathrin-independent carriers, with possible implications for disease development.

Previous in vitro studies showed that GRAF1 harbours a GTPase activating domain to inactivate Rho GTPase Cdc42, a major actin cytoskeleton regulator. Herein, microscopy based approaches used to analyse HeLa cells demonstrated the importance of a transient interaction between GRAF1 and Cdc42 for proper processing of GRAF1-decorated carriers. Although GRAF1-mediated inactivation of Cdc42 was not vital for the budding of carriers from the plasma membrane, it was important for carrier maturation. In addition, studies of purified GRAF1 and its association with lipid bilayers identified a membrane scaffolding-dependent oligomerisation mechanism, with the ability to sculpt membranes. This was consistent with the assumption that GRAF1 possesses an inherent banana shaped membrane binding domain. Remarkably, this function was autoinhibited and in direct competition with the Cdc42 interaction domain.

Finally, other novel GRAF1 interaction partners were identified in this study. Interestingly, many of these partners are known to be associated with protein complexes involved in cell adherence, spreading and migration. Although never actually seen localising to mature focal adhesions that anchor cells to their growth surface, dynamic GRAF1 carriers were captured travelling to and from such locations. Moreover, GRAF1 was recruited specifically to smaller podosome-like structures. Consistent with this, the tracking of GRAF1 in live cells uncovered a clear pattern of dynamic carrier formation at sites of active membrane turnover – notably protrusions at the cell periphery. Furthermore, the silencing of GRAF1 gave rise to cells defective in spreading and migration, indicating a targeting of GRAF1-mediated endocytosis to aid in rapid plasma membrane turnover needed for morphological changes that are a prerequisite for cell movement. Since these cells exhibited an increase in active Rab8, a GTPase responsible for polarised vesicle transport, the phenotype could also be explained by a defect in Rab8 trafficking that results in hyperpolarisation.

Taken together, the spatial and temporal regulation of GRAF1 membrane sculpting function is likely to be accomplished via its membrane binding propensity, in concert with various protein interactions. The importance of GRAF1 in aiding membrane turnover during cell movement spans different functional levels – from its local coordination of membrane and actin dynamics by interacting with Cdc42, to its global role in membrane lipid trafficking.

Place, publisher, year, edition, pages
Umeå: Umeå University, 2015. p. 62
Series
Umeå University medical dissertations, ISSN 0346-6612 ; 1761
Keywords
Endocytosis, migration, polarisation, tension, CLIC/GEEC, GRAF1, Rho GTPase, Cdc42, Rab8
National Category
Cell and Molecular Biology
Research subject
Medical Biochemistry
Identifiers
urn:nbn:se:umu:diva-111213 (URN)978-91-7601-377-9 (ISBN)
Public defence
2015-12-04, N300, Naturvetarhuset, Umeå, 09:00 (English)
Opponent
Supervisors
Available from: 2015-11-13 Created: 2015-11-10 Last updated: 2018-06-07Bibliographically approved
Amer, A., Åhlund, M., Bröms, J., Forsberg, Å. & Francis, M. (2011). Impact of the N-terminal secretor domain on YopD translocator function in Yersinia pseudotuberculosis type III secretion. Journal of Bacteriology, 193(23), 6683-6700
Open this publication in new window or tab >>Impact of the N-terminal secretor domain on YopD translocator function in Yersinia pseudotuberculosis type III secretion
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2011 (English)In: Journal of Bacteriology, ISSN 0021-9193, E-ISSN 1098-5530, Vol. 193, no 23, p. 6683-6700Article in journal (Refereed) Published
Abstract [en]

Type III secretion systems (T3SSs) secrete needle components, pore-forming translocators, and the translocated effectors. In part, effector recognition by a T3SS involves their N-terminal amino acids and their 5′ mRNA. To investigate whether similar molecular constraints influence translocator secretion, we scrutinized this region within YopD from Yersinia pseudotuberculosis. Mutations in the 5′ end of yopD that resulted in specific disruption of the mRNA sequence did not affect YopD secretion. On the other hand, a few mutations affecting the protein sequence reduced secretion. Translational reporter fusions identified the first five codons as a minimal N-terminal secretion signal and also indicated that the YopD N terminus might be important for yopD translation control. Hybrid proteins in which the N terminus of YopD was exchanged with the equivalent region of the YopE effector or the YopB translocator were also constructed. While the in vitro secretion profile was unaltered, these modified bacteria were all compromised with respect to T3SS activity in the presence of immune cells. Thus, the YopD N terminus does harbor a secretion signal that may also incorporate mechanisms of yopD translation control. This signal tolerates a high degree of variation while still maintaining secretion competence suggestive of inherent structural peculiarities that make it distinct from secretion signals of other T3SS substrates.

Place, publisher, year, edition, pages
American Society for Microbiology, 2011
Keywords
mRNA, amphipathic, effector, hierarchy, translation, chaperone
National Category
Biological Sciences Microbiology in the medical area
Research subject
Infectious Diseases; Microbiology
Identifiers
urn:nbn:se:umu:diva-49681 (URN)10.1128/JB.00210-11 (DOI)
Funder
Swedish Research Council, 2009-5628
Available from: 2011-11-16 Created: 2011-11-15 Last updated: 2018-06-08Bibliographically approved
Doherty, G. J., Åhlund, M. K., Howes, M. T., Moren, B., Parton, R. G., McMahon, H. T. & Lundmark, R. (2011). The endocytic protein GRAF1 is directed to cell-matrix adhesion sites and regulates cell spreading. Molecular Biology of the Cell, 22(22), 4380-4389
Open this publication in new window or tab >>The endocytic protein GRAF1 is directed to cell-matrix adhesion sites and regulates cell spreading
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2011 (English)In: Molecular Biology of the Cell, ISSN 1059-1524, E-ISSN 1939-4586, Vol. 22, no 22, p. 4380-4389Article in journal (Refereed) Published
Abstract [en]

The rho GTPase-activating protein GTPase regulator associated with focal adhesion kinase-1 (GRAF1) remodels membranes into tubulovesicular clathrin-independent carriers (CLICs) mediating lipid-anchored receptor endocytosis. However, the cell biological functions of this highly prevalent endocytic pathway are unclear. In this article, we present biochemical and cell biological evidence that GRAF1 interacted with a network of endocytic and adhesion proteins and was found enriched at podosome-like adhesions and src-induced podosomes. We further demonstrate that these sites comprise microdomains of highly ordered lipid enriched in GRAF1 endocytic cargo. GRAF1 activity was upregulated in spreading cells and uptake via CLICs was concentrated at the leading edge of migrating cells. Depletion of GRAF1, which inhibits CLIC generation, resulted in profound defects in cell spreading and migration. We propose that GRAF1 remodels membrane microdomains at adhesion sites into endocytic carriers, facilitating membrane turnover during cell morphological changes.

Place, publisher, year, edition, pages
Bethesda: American Society for Cell Biology, 2011
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-50518 (URN)10.1091/mbc.E10-12-0936 (DOI)000297164200017 ()
Available from: 2011-12-13 Created: 2011-12-13 Last updated: 2018-06-08Bibliographically approved
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