Structural insights into the small GTPase specificity of the DOCK guanine nucleotide exchange factors |
| |
| Institution: | 1. Immunology Department, Great Ormond Street Hospital, Great Ormond Street, London WC1N 3JH, UK;2. Paediatric Centre for Hepatology, Gastroenterology and Nutrition, King''s College Hospital, Denmark Hill, London SE5 9RS, UK;1. Department of Pharmacology,CINVESTAV-IPN,México D.F.,Mexico;2. Department of Cell Biology,CINVESTAV-IPN,México D.F.,Mexico;3. Department of Molecular, Cell, and Developmental Biology and Molecular Biology Institute,University of California,Los Angeles, CA,USA |
| |
| Abstract: | The dedicator of cytokinesis (DOCK) family of guanine nucleotide exchange factors (GEFs) regulates cytoskeletal dynamics by activating the GTPases Rac and/or Cdc42. Eleven human DOCK proteins play various important roles in developmental processes and the immune system. Of these, DOCK1–5 proteins bind to engulfment and cell motility (ELMO) proteins to perform their physiological functions. Recent structural studies have greatly enhanced our understanding of the complex and diverse mechanisms of DOCK GEF activity and GTPase recognition and its regulation by ELMO. This review is focused on gaining structural insights into the substrate specificity of the DOCK GEFs, and discuss how Rac and Cdc42 are specifically recognized by the catalytic DHR-2 and surrounding domains of DOCK or binding partners. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
