CrkIII: a novel and biologically distinct member of the Crk family of adaptor proteins. Oncogene 2003 Jul 31;22(31):4799-806
Date
08/02/2003Pubmed ID
12894221DOI
10.1038/sj.onc.1206714Scopus ID
2-s2.0-0042567278 (requires institutional sign-in at Scopus site) 26 CitationsAbstract
As the role for adaptor proteins constantly proliferates, appreciation of their importance has never been higher. The Crk family of adaptor proteins is no exception. Currently comprising four members, v-Crk, CrkI, CrkII and Crk-like protein, we have introduced a fifth member, CrkIII. Cloned by the CORT technique, CrkIII is identical in sequence to CrkII until the second of its two SH3 domains, which is disrupted partway through and results in a nonfunctional domain and a unique C-terminal sequence. We have demonstrated the existence of native CrkIII at the message level using RT-PCR and RNAse protection assays, and at the protein level in mouse fibroblasts. We show that CrkII overexpression is capable of enhancing insulin-stimulated ERK activity, whereas CrkIII is not, thus partially characterizing a novel member of the Crk family and elucidating important effects mediated by the c-terminal SH3 domain.
Author List
Prosser S, Sorokina E, Pratt P, Sorokin AAuthor
Andrey Sorokin PhD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular Transport
Amino Acid Sequence
Animals
Cell Line
Cells, Cultured
Cloning, Molecular
Gene Expression Regulation
Gene Library
Genetic Vectors
Glomerular Mesangium
Humans
Insulin
Mastadenovirus
Mice
Mitogen-Activated Protein Kinase 1
Mitogen-Activated Protein Kinase 3
Mitogen-Activated Protein Kinases
Molecular Sequence Data
Multigene Family
Mutagenesis, Site-Directed
Protein Isoforms
Protein Structure, Tertiary
Proto-Oncogene Proteins
Proto-Oncogene Proteins c-crk
Recombinant Fusion Proteins
Sequence Alignment
Sequence Homology, Amino Acid
Transfection
src Homology Domains
