Characterization of interactions of Nck with Sos and dynamin

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

One of the adaptor proteins, Nck, comprises a single SH2 domain and three SH3 domains that are important in protein-protein interactions. The in vivo association of Nck with the guanine nucleotide exchange factor Sos has been well documented; however, the precise nature of the interaction is unclear. To determine which SH3 domains are involved in the Nck-Sos interaction, individual SH3 domains of Nck were generated as glutathione S-transferase fusion proteins. We found that exclusively the third (C-terminal) SH3 domain of Nck has the ability to bind to Sos. In addition, in [35S]methionine labelled K562 cells, a 100,000 M(r) protein was found to be associated with the third SH3 domain of Nck. This protein was identified as dynamin, a GTP-binding protein that has been implicated in clathrin-coated vesicle formation. Dynamin and Nck co-precipitated when cell lysates were immunoprecipitated with anti-Nck antibody. These data suggest that Nck may contribute to Ras activation and the function of dynamin in membrane trafficking through its third SH3 domain. Copyright (C) 1998 Elsevier Science Inc.

Original languageEnglish
Pages (from-to)25-29
Number of pages5
JournalCellular Signalling
Volume11
Issue number1
DOIs
Publication statusPublished - Jan 1999

Fingerprint

Dynamins
src Homology Domains
Proteins
Clathrin-Coated Vesicles
Guanine Nucleotide Exchange Factors
K562 Cells
Glutathione Transferase
GTP-Binding Proteins
Methionine
Anti-Idiotypic Antibodies
Membranes

Keywords

  • Dynamin
  • K562 cells
  • Nck
  • SH2/SH3 domains
  • Sos

ASJC Scopus subject areas

  • Cell Biology

Cite this

Characterization of interactions of Nck with Sos and dynamin. / Wunderlich, L.; Faragó, A.; Buday, L.

In: Cellular Signalling, Vol. 11, No. 1, 01.1999, p. 25-29.

Research output: Contribution to journalArticle

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