Molecular analysis of pleckstrin: the major protein kinase C substrate of platelets.

摘要: Activation of protein kinase C (PKC) in platelets causes the immediate phosphorylation pleckstrin, an apparent Mr 40-47,000 previously called 40K or P47. Pleckstrin presumably plays important but as yet unknown role mediating cellular responses evoked by agonist-induced phosphoinositide turnover. We have cloned cDNA for pleckstrin from HL-60 human promyelocytic leukemia cell line immunological screening a lambda gt11 expression library (Tyers et al.: Nature 333:470-473, 1988) and now report further analysis sequence. has deduced 40,087 is encoded 1,050-bp open reading frame which preceded short that terminates before correct initiator methionine. A single polymorphic site was found coding region. An unusual pattern sequence heterogeneity occurred about poly(A) tract 3' untranslated The 3.0-kb mRNA induced upon differentiation cells apparently heterogeneous 5' ends undergo differential regulation during maturation. Analysis multiple alignment with known PKC substrates identified strong candidate potential Ca2+-binding EF-hand motif. No other similarities to proteins current databases were found.