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Ubiquitin C-terminal hydrolase-L1 interacts with adhesion complexes and promotes cell migration, survival, and anchorage independent growth
Department of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.ORCID iD: 0000-0002-1209-0942
2012 (English)In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 26, no 12, p. 5060-5070Article in journal (Refereed) Published
Abstract [en]

Ubiquitin C-terminal hydrolase-L1 (UCH-L1) is a deubiquitinating enzyme of unknown function that is highly expressed in neurons and overexpressed in several human cancers. UCH-L1 has been implicated in the regulation of phenotypic properties associated with malignant cell growth but the underlying mechanisms have not been elucidated. By comparing cells expressing catalytically active or inactive versions of UCH-L1, we found that the active enzyme enhances cell adhesion, spreading, and migration; inhibits anoikis; and promotes anchorage independent growth. UCH-L1 accumulates at the motile edge of the cell membrane during the initial phases of adhesion, colocalizes with focal adhesion kinase (FAK), p120-catenin, and vinculin, and enhances the formation of focal adhesions, which correlates with enhanced FAK activation. The involvement of UCH-L1 in the regulation of focal adhesions and adherens junctions is supported by coimmunoprecipitation with key components of these complexes, including FAK, paxillin, p120-catenin, β-catenin, and vinculin. UCH-L1 stabilizes focal adhesion signaling in the absence of adhesion, as assessed by reduced caspase-dependent cleavage of FAK following cell detachment and sustained activity of the AKT signaling pathway. These findings offer new insights on the molecular interactions through which the deubiquitinating enzyme regulates the survival, proliferation, and metastatic potential of malignant cells.

Place, publisher, year, edition, pages
The Federation of American Societies for Experimental Biology , 2012. Vol. 26, no 12, p. 5060-5070
National Category
Cell and Molecular Biology Cancer and Oncology Cell Biology Microbiology
Identifiers
URN: urn:nbn:se:umu:diva-165142DOI: 10.1096/fj.12-211946ISI: 000311838300027PubMedID: 22932395OAI: oai:DiVA.org:umu-165142DiVA, id: diva2:1369409
Available from: 2019-11-12 Created: 2019-11-12 Last updated: 2019-11-12Bibliographically approved

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Frisan, Teresa

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