Characterization of VIK-1: a new Vav-interacting Kruppel-like protein.

Binding partners of the Src homology domains of Vav-1 were characterized by a two-hybrid screening of a Jurkat cell cDNA library. One of the isolated clones encoded a new protein named VIK that belongs to the Kruppel-like zinc-finger gene family. Genome mapping showed that a single gene positioned at chromosome ...
7q22.1 generated three possible isoforms containing alternative domains such as proline-rich and Kruppel-associated box A or B repressor domains. The isolated isoform, VIK-1, did not contain such motifs but presented six tandemly arranged zinc-fingers and consensus Kruppel H-C links. VIK-1 interacted both with Vav-1 and cyclin-dependent kinase 4 through two independent domains and corresponded to a Vav C-Src homology domain (SH)3 partner able to shuttle between the nucleus and the cytoplasm exhibiting functional nuclear addressing and export sequences. The results indicated a restricted expression of the protein during the G1 phase and its overexpression resulted in an inhibition of the cell-cycle progression that was reversed in the presence of Vav 1. Thus, this ubiquitous factor provides a first link between Vav-1 and the cell-cycle machinery.
Mesh Terms:
Amino Acid Sequence, Carrier Proteins, Cell Cycle, Cell Nucleus, Cyclin-Dependent Kinase 4, Cyclin-Dependent Kinases, Cytoplasm, Fungal Proteins, Humans, Jurkat Cells, Kruppel-Like Transcription Factors, Microtubule-Associated Proteins, Molecular Sequence Data, Nuclear Localization Signals, Oncogene Proteins, Protein Binding, Protein Structure, Tertiary, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-vav
Oncogene
Date: Jan. 06, 2005
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