The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves Ras through an atypical mechanism to disrupt Ras-ERK signaling-Reference-Cited by-同舟云学术

The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves Ras through an atypical mechanism to disrupt Ras-ERK signaling

Published:2018-10-02 Issue:550 Volume:11 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Biancucci Marco¹,Minasov George¹²^ORCID,Banerjee Avik³^ORCID,Herrera Alfa¹^ORCID,Woida Patrick J.¹^ORCID,Kieffer Matthew B.¹^ORCID,Bindu Lakshman⁴,Abreu-Blanco Maria⁴,Anderson Wayne F.²⁵^ORCID,Gaponenko Vadim⁶,Stephen Andrew G.⁴,Holderfield Matthew⁴^ORCID,Satchell Karla J. F.¹²^ORCID

Affiliation:

1. Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.

2. Center for Structural Genomics of Infectious Diseases, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.

3. Department of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA.

4. National Cancer Institute-RAS Initiative, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Leidos Biomedical Research, Frederick, MD 21702, USA.

5. Department of Biochemistry and Molecular Genetics, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.

6. Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607, USA.

Abstract

A bacterial toxin effector domain disrupts RAS-ERK signaling by cleaving RAS through an unusual mechanism.

Funder

U.S. Department of Defense

National Cancer Institute

National Institute of Allergy and Infectious Diseases

Chicago biomedical consortium

Pancreatic Cancer Action Network

National Institute of Arthritis and Musculoskeletal and Skin Diseases

Robert H. Lurie Comprehensive Cancer Center