Specific Disruption of Ras2 CAAX Proteolysis Alters Its Localization and Function-Reference-Cited by-同舟云学术

Specific Disruption of Ras2 CAAX Proteolysis Alters Its Localization and Function

Published:2023-02-14 Issue:1 Volume:11 Page:
ISSN:2165-0497
Container-title:Microbiology Spectrum
language:en
Short-container-title:Microbiol Spectr

Author:

Ravishankar Rajani¹^ORCID,Hildebrandt Emily R.¹,Greenway Grace¹,Asad Nadeem²,Gore Sangram²,Dore Timothy M.²³,Schmidt Walter K.¹^ORCID

Affiliation:

1. Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA

2. New York University Abu Dhabi, Abu Dhabi, United Arab Emirates

3. Department of Chemistry, University of Georgia, Athens, Georgia, USA

Abstract

CAAX proteins are subject to multiple posttranslational modifications: cysteine prenylation, CAAX proteolysis, and carboxylmethylation. For investigations of CAAX proteolysis, this study took the novel approach of using a proteolysis-resistant CAAX sequence to stage Saccharomyces cerevisiae Ras2 GTPase in a farnesylated and nonproteolyzed state.

Funder

New York University Abu Dhabi

HHS | NIH | National Institute of General Medical Sciences

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Cell Biology,Microbiology (medical),Genetics,General Immunology and Microbiology,Ecology,Physiology

Link

https://journals.asm.org/doi/pdf/10.1128/spectrum.02692-22

Reference62 articles.

1. Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage

2. TheSaccharomyces cerevisiaePrenylcysteine Carboxyl Methyltransferase Ste14p Is in the Endoplasmic Reticulum Membrane