High impact information on STK10

• Phosphopeptide mapping and phosphoamino acid analyses of Plk labeled in vivo and phosphorylated in vitro by Xenopus polo-like kinase kinase-1 (xPlkk1) or by lymphocyte-oriented kinase, its most closely related mammalian enzyme, indicate that Thr-210 is a major phosphorylation site in activated Plk from mitotic HeLa cells [1].
• LOK phosphorylated itself as well as substrates such as myelin basic protein and histone IIA on serine and threonine residues but not on tyrosine residues, establishing LOK as a novel serine/threonine kinase [2].
• These results suggest that LOK could be involved in a novel signaling pathway in lymphocytes, which is distinct from the known MAP kinase cascades [2].
• Our results show a remarkably low mutation frequency, with only a single somatic point mutation, a K277E mutation in the STK10 gene, being identified in a total of more than 15 megabases of sequence analyzed [3].
• Opposing roles of serine/threonine kinases MEKK1 and LOK in regulating the CD28 responsive element in T-cells [4].

Biological context of STK10

• These results established STK10 as a new marker of human chromosome 5 to define the syntenic boundary of human chromosomes 5 and 16 on mouse chromosome 11 [5].
• The amino acid sequence deduced from the cDNA shows a high similarity to that of mouse LOK, with 88% identity as a whole [5].
• GLEM/LOK report on proctology practice in Belgium. Results, comments and recommendations [6].

Regulatory relationships of STK10

• These data suggest that MEKK1 and LOK may have opposing roles in regulating the CD28RE/AP1 element [4].

Other interactions of STK10

• Three of these genes (glucokinase, serine-threonine kinase 10 and cRAF) were confirmed as stress-responsive using real-time PCR [7].

Analytical, diagnostic and therapeutic context of STK10

• Western blot analysis with mouse LOK-specific antibody detected 130 000 Mr LOK proteins in human and rat lymphoid cell lines and tissues [5].

References