Characterization of Interactions of Nck with Sos and Dynamin
作者： Livius Wunderlich , Anna Faragó , László Buday
DOI: 10.1016/S0898-6568(98)00027-8
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摘要: Abstract One of the adaptor proteins, Nck, comprises a single SH2 domain and three SH3 domains that are important in protein–protein interactions. The vivo association Nck with guanine nucleotide exchange factor Sos has been well documented; however, precise nature interaction is unclear. To determine which involved Nck–Sos interaction, individual were generated as glutathione S-transferase fusion proteins. We found exclusively third (C-terminal) ability to bind Sos. In addition, [35S]methionine labelled K562 cells, 100,000 Mr protein was be associated Nck. This identified dynamin, GTP-binding implicated clathrin-coated vesicle formation. Dynamin co-precipitated when cell lysates immunoprecipitated anti-Nck antibody. These data suggest may contribute Ras activation function dynamin membrane trafficking through its domain.
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