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Characterization of MYR1, a dosage suppressor of YPT6 and RIC1 deficient mutants
Umeå University, Faculty of Science and Technology, Chemistry.
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2008 (English)In: Current Genetics, ISSN 0172-8083, E-ISSN 1432-0983, Vol. 53, no 4, 235-47 p.Article in journal (Refereed) Published
Abstract [en]

Membrane traffic is tightly regulated and the Rab protein family of small GTPases plays a central role in this regulation. One member of this family is the Saccharomyces cerevisae protein Ypt6. To search for new genes interacting with Ypt6-related pathways, we performed a genetic screen for high copy suppressors of ypt6Delta temperature sensitivity at 35 degrees C. Among the suppressors, MYR1 was also able to suppress the temperature sensitive mutant lacking Ric1, a subunit of the Ypt6 guanine exchanging factor complex Ric1/Rgp1. Myr1 is characterized by a coiled coil region and a GYF domain, a protein module binding proline-rich sequences. Myr1 is able to bind membranes but is also associated with larger structures insoluble in Triton X-100. By immunofluorescence, Myr1 shows a network-like pattern as well as small foci. Overexpression of Myr1 influences nuclear envelope morphology and high levels are lethal. This lethality is rescued when the N-terminal region, containing the GYF domain, is deleted. The transcription profile of a myr1Delta strain shows effects on genes involved in nuclear migration, Ras signalling and transcription. Taken together, these results suggest that Myr1 is a novel factor linked to the secretory pathway and important cellular regulatory mechanisms.

Place, publisher, year, edition, pages
Berlin: Springer , 2008. Vol. 53, no 4, 235-47 p.
Keyword [en]
Ypt6, Ric1, GYF domain, Membrane traffic, Coiled coil, Yeast, Myr1
Identifiers
URN: urn:nbn:se:umu:diva-20492DOI: 10.1007/s00294-008-0183-0PubMedID: 18327588OAI: oai:DiVA.org:umu-20492DiVA: diva2:208800
Available from: 2009-03-20 Created: 2009-03-20 Last updated: 2017-12-13Bibliographically approved

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