Literature DB >> 1904369

The localization of the cAMP-dependent protein kinase phosphorylation site in the platelet rat protein, rap 1B.

T H Fischer1, J H Collins, M N Gatling, G C White.   

Abstract

Rap 1B is a low molecular weight G protein which is phosphorylated by cAMP-dependent protein kinase. In order to identify the site of phosphorylation by cAMP-dependent protein kinase, purified rap 1B from human platelets was phosphorylated and subjected to limited proteolysis with trypsin. Single digestion fragment containing the phosphorylation site was obtained and purified by reversed-phase HPLC. Sequence analysis of the phosphorylated digestion fragment demonstrated that the sequence of the phosphorylation site was -Lys-Lys-Ser-Ser-. This sequence is near the carboxy terminus and is adjacent to the site of membrane attachment of the protein.

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Year:  1991        PMID: 1904369     DOI: 10.1016/0014-5793(91)80581-m

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Protein kinase A-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration.

Authors:  Maho Takahashi; Tara J Dillon; Chang Liu; Yumi Kariya; Zhiping Wang; Philip J S Stork
Journal:  J Biol Chem       Date:  2013-08-14       Impact factor: 5.157

2.  Phosphorylation of Rap1 by cAMP-dependent Protein Kinase (PKA) Creates a Binding Site for KSR to Sustain ERK Activation by cAMP.

Authors:  Maho Takahashi; Yanping Li; Tara J Dillon; Philip J S Stork
Journal:  J Biol Chem       Date:  2016-12-21       Impact factor: 5.157

  2 in total

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