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Molecular cloning of protein phosphatase inhibitor-1 and its expression in rat and rabbit tissues.

Authors: Elbrecht, A  DiRenzo, J  Smith, RG  Shenolikar, S 
Citation: Elbrecht A, etal., J Biol Chem 1990 Aug 15;265(23):13415-8.
Pubmed: (View Article at PubMed) PMID:1696252

A cDNA encoding the complete amino acid sequence of rat protein phosphatase inhibitor-1 was obtained by screening a skeletal muscle library. The coding region represents a 171-residue polypeptide which demonstrated 80% overall identity with the primary sequence of rabbit inhibitor-1. Sequence homology between the rat and rabbit proteins was particularly striking (98% identity) in the NH2-terminal 61 amino acids, which encompass the threonine phosphorylated by cyclic AMP-dependent protein kinase. This domain possesses full inhibitor activity against type-1 protein phosphatases. In contrast, a domain of similar size at the COOH terminus showed only 57% conservation of primary structure between the two proteins. This reflects a remarkable difference in evolutionary pressures experienced by these domains and may emphasize a lesser role for the COOH-terminal region in inhibitor-1 function. Northern hybridization analysis of RNA from rat and rabbit tissues indicated the presence of two mRNAs, a major 0.7-kilobase and a minor 1.8-kilobase mRNA. The highest expression of inhibitor-1 mRNA was noted in skeletal muscle from both species. Analysis of mRNA levels illustrates potential post-transcriptional mechanisms controlling inhibitor-1 expression in some mammalian tissues.


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RGD Object Information
RGD ID: 61702
Created: 2001-04-10
Species: All species
Last Modified: 2001-04-10
Status: ACTIVE


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