| First Author | Malek SN | Year | 1994 |
| Journal | J Biol Chem | Volume | 269 |
| Issue | 52 | Pages | 33009-20 |
| PubMed ID | 7528743 | Mgi Jnum | J:40217 |
| Mgi Id | MGI:87559 | Doi | 10.1016/s0021-9258(20)30091-0 |
| Citation | Malek SN, et al. (1994) A cyclin-dependent kinase homologue, p130PITSLRE is a phosphotyrosine-independent SH2 ligand. J Biol Chem 269(52):33009-20 |
| abstractText | Src-homology 2 (SH2) domains are conserved, globular protein modules that mediate assembly of multicomponent signaling complexes. Phosphoproteins from the B-lymphoid cell line A20 were isolated by SH2 affinity chromatography; the peptide sequence from one of these proteins was used to molecularly clone several related complementary DNAs whose predominant protein product, p130PITSLRE, is an abundant serine/threonine kinase with ubiquitous expression in murine tissues. The sequence of a previously described cyclin-dependent kinase homologue, p58clk-1, is entirely contained within the p130PITSLRE sequence. Specific binding of p130PITSLRE to SH2 domains is mediated by a serine- and glutamic acid-rich cluster of amino acids in the N-terminal region. This interaction is dependent on serine/threonine phosphorylation but independent of tyrosine phosphorylation. Binding is inhibited by free phosphotyrosine and by a phosphotyrosine-containing peptide from polyoma middle T antigen, suggesting that the p130PITSLRE binding site in the SH2 domain overlaps the region that binds phosphotyrosine-containing peptides. Bacterially expressed p130PITSLRE fragments acquire the ability to bind an SH2 domain when phosphorylated in vitro with casein kinase II. A subset of casein kinase II phosphorylation sites may therefore constitute a phosphotyrosine-independent class of SH2 ligands. |
