Faculty Collaboration Database

She3p possesses a novel activity required for ASH1 mRNA localization in Saccharomyces cerevisiae. Eukaryot Cell 2009 Jul;8(7):1072-83

Date

05/12/2009

Pubmed ID

19429778

Pubmed Central ID

PMC2708451

DOI

10.1128/EC.00084-09

Scopus ID

2-s2.0-67650457062 (requires institutional sign-in at Scopus site)   15 Citations

Abstract

Intracellular and intercellular polarity requires that specific proteins be sorted to discreet locations within and between cells. One mechanism for sorting proteins is through RNA localization. In Saccharomyces cerevisiae, ASH1 mRNA localizes to the distal tip of the bud, resulting in the asymmetric sorting of the transcriptional repressor Ash1p. ASH1 mRNA localization requires four cis-acting localization elements and the trans-acting factors Myo4p, She3p, and She2p. Myo4p is a type V myosin motor that functions to directly transport ASH1 mRNA to the bud. She2p is an RNA-binding protein that directly interacts with the ASH1 mRNA cis-acting elements. Currently, the role for She3p in ASH1 mRNA localization is as an adaptor protein, since it can simultaneously associate with Myo4p and She2p. Here, we present data for two novel mutants of She3p, S348E and the double mutant S343E S361E, that are defective for ASH1 mRNA localization, and yet both of these mutants retain the ability to associate with Myo4p and She2p. These observations suggest that She3p possesses a novel activity required for ASH1 mRNA localization, and our data imply that this function is related to the ability of She3p to associate with ASH1 mRNA. Interestingly, we determined that She3p is phosphorylated, and global mass spectrometry approaches have determined that Ser 343, 348, and 361 are sites of phosphorylation, suggesting that the novel function for She3p could be negatively regulated by phosphorylation. The present study reveals that the current accepted model for ASH1 mRNA localization does not fully account for the function of She3p in ASH1 mRNA localization.

Author List

Landers SM, Gallas MR, Little J, Long RM

Author

Roy M. Long PhD Assistant Dean, Associate Professor in the Medical School Regional Campuses department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Biological Transport
Catalytic Domain
Cell Polarity
Cytoplasm
Gene Expression Regulation, Fungal
Mass Spectrometry
Mutation
Myosin Heavy Chains
Myosin Type V
Nuclear Proteins
Phosphorylation
Protein Binding
Protein Biosynthesis
Protein Transport
RNA Transport
RNA, Messenger
RNA-Binding Proteins
Regulatory Elements, Transcriptional
Repressor Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Trans-Activators
Transcriptional Activation