Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Recently we reported that osmotic shock increased the insulin-stimulated tyrosine phosphorylation of a 68-kDa RNA-binding protein in 3T3-L1 adipocytes (Hresko, R. C., and Mueckler, M. (2000) J. Biol. Chem. 275, 18114-18120). In this present study we have identified, by MALDI mass spectrometry, pp68 as the tyrosine-phosphorylated form of synaptotagmin-binding cytoplasmic RNA-interacting protein (SYNCRIP)/NSAP1, a newly discovered cytoplasmic RNA-binding protein. Both SYNCRIP and pp68 were enriched in free polysomes found in low density microsomes isolated from 3T3-L1 adipocytes. In vitro phosphorylation studies revealed that SYNCRIP, once extracted from low density microsomes, can be tyrosine phosphorylated using purified insulin receptor. Binding of RNA to SYNCRIP specifically inhibited its in vitro phosphorylation but had no effect on receptor autophosphorylation or on the ability of the receptor to phosphorylate a model substrate, RCM-lysozyme. These results raise the possibility that regulation of mRNA translation or stability by insulin may involve the phosphorylation of SYNCRIP.
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PMID:Identification of pp68 as the Tyrosine-phosphorylated Form of SYNCRIP/NSAP1. A cytoplasmic RNA-binding protein. 1199 98