Characterization of MYR1, a dosage suppressor of YPT6 and RIC1 deficient mutants.

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.
Mesh Terms:
Amino Acid Sequence, Carrier Proteins, Cell Membrane, Cell Nucleus Shape, Conserved Sequence, Guanine Nucleotide Exchange Factors, Membrane Proteins, Monomeric GTP-Binding Proteins, Octoxynol, Protein Structure, Tertiary, Protein Transport, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Deletion, Signal Transduction, Solubility, Suppression, Genetic, Transcription Factors, ras Proteins
Curr. Genet.
Date: Apr. 01, 2008
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