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PMID: 11481476 Published · ppublish English Journal Article

The sorbin homology domain: a motif for the targeting of proteins to lipid rafts.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 98 ·No. 16 ·2001-07-31 ·Pages 9098-103

Kimura A, Baumann CA, Chiang SH, Saltiel AR

Abstract

On phosphorylation of Cbl, the c-Cbl-associated protein (CAP)/Cbl complex dissociates from the insulin receptor and translocates to a lipid raft membrane fraction to form a ternary complex with flotillin. Deletion analyses of the CAP gene identified a 115-aa region responsible for flotillin binding. This region is homologous to the peptide sorbin and is referred to as the sorbin homology (SoHo) domain. This domain is present in two other proteins, vinexin and ArgBP2. Vinexin also interacted with flotillin, and deletion of its SoHo domain similarly blocked flotillin binding. The overexpression of a CAP mutant in which the SoHo domain had been deleted (CAPDeltaSoHo) prevented the translocation of Cbl to lipid rafts and subsequently blocked the recruitment of CrkII and C3G. Moreover, overexpression of CAPDeltaSoHo prevented the stimulation of glucose transport and GLUT4 translocation by insulin. These results suggest a mechanism for localization of signaling proteins to the lipid raft that mediates the compartmentalization of crucial signal transduction pathways.

MeSH Terms
3T3 Cells Amino Acid Motifs Amino Acid Sequence Animals Base Sequence Cell Line DNA Primers Glucose/metabolism Humans Insulin/pharmacology Lipid Metabolism Mice Molecular Sequence Data Peptides/chemistry Phosphorylation Protein Transport Proto-Oncogene Proteins/chemistry,metabolism Proto-Oncogene Proteins c-cbl Sequence Homology, Amino Acid Ubiquitin-Protein Ligases
Chemicals
DNA Primers Insulin Peptides Proto-Oncogene Proteins sorbin peptide Proto-Oncogene Proteins c-cbl Ubiquitin-Protein Ligases CBL protein, human Cbl protein, mouse Glucose
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kimura A
Department of Internal Medicine and Physiology, Life Sciences Institute, University of Michigan Medical Center, Ann Arbor, MI 48109, USA.
Baumann C A
Chiang S H
Saltiel A R
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.151252898
Published
2001-07-31
Pages
9098-103
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC55379
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.151252898 PMC Full Text View journal details
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