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Characterization of MYR1, a dosage suppressor of YPT6 and RIC1 deficient mutants
Södertörn University, School of Life Sciences, Biology. Stockholm University.
Umeå University.
Södertörn University, School of Life Sciences, Biology.
Södertörn University, School of Life Sciences, Biology.
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2008 (English)In: Current Genetics, ISSN 0172-8083, E-ISSN 1432-0983, Vol. 53, no 4, 235-247 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 ypt6 Delta 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 myr1 Delta 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
2008. Vol. 53, no 4, 235-247 p.
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:sh:diva-17359DOI: 10.1007/s00294-008-0183-0ISI: 000254182700005Scopus ID: 2-s2.0-41149157331OAI: oai:DiVA.org:sh-17359DiVA: diva2:570788
Available from: 2012-11-20 Created: 2012-11-19 Last updated: 2017-02-13Bibliographically approved
In thesis
1. Functional studies of nuclear envelope-associated proteins in Saccharomyces cerevisiae
Open this publication in new window or tab >>Functional studies of nuclear envelope-associated proteins in Saccharomyces cerevisiae
2008 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Proteins of the nuclear envelope play important roles in a variety of cellular processes e.g. transport of proteins between the nucleus and cytoplasm, co-ordination of nuclear and cytoplasmic events, anchoring of chromatin to the nuclear periphery and regulation of transcription. Defects in proteins of the nuclear envelope and the nuclear pore complexes have been related to a number of human diseases. To understand the cellular functions in which nuclear envelope proteins participate it is crucial to map the functions of these proteins.

The present study was done in order to characterize the role of three different proteins in functions related to the nuclear envelope in the yeast Saccharomyces cerevisiae. The arginine methyltransferase Rmt2 was demonstrated to associate with proteins of the nuclear pore complexes and to influence nuclear export. In addition, Rmt2 was found to interact with the Lsm4 protein involved in RNA degradation, splicing and ribosome biosynthesis. These results provide support for a role of Rmt2 at the nuclear periphery and potentially in nuclear transport and RNA processing. The integral membrane protein Cwh43 was localized to the inner nuclear membrane and was also found at the nucleolus. A nuclear function for Cwh43 was demonstrated by its ability to bind DNA in vitro. A link to nucleolar functions was demonstrated by genetic analysis. Furthermore, Cwh43 is interacting with signalling pathways perhaps acting as a sensor for signals transmitted from the cytoplasm to the nucleus. The Myr1 protein was found to be membrane-associated and to interact with proteins involved in vesicular traffic. Overexpression of Myr1 affects nuclear morphology and nuclear pore distribution suggesting a function in membrane dynamics.

In conclusion, the presented results aid in a deeper understanding of functions related to the nuclear envelope in revealing a novel link between arginine methylation and the nuclear periphery, identifying a novel inner nuclear membrane protein and a new membrane-associated protein.

Place, publisher, year, edition, pages
Stockholm: Department of Biochemistry and Biophysics, Stockholm university, 2008. 58 p.
Keyword
Nucleus, nuclear envelope, nuclear pore complexes, vesicular traffic, arginine methylation, Rmt2, Cwh43, Myr1
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:sh:diva-32040 (URN)978-91-7155-666-0 (ISBN)
Public defence
2008-05-29, MA 636, Alfred Nobels allé 7, Huddinge, 13:00 (English)
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Available from: 2017-02-13 Created: 2017-02-13 Last updated: 2017-02-13Bibliographically approved

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