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Cvak104 is a novel poly-l-lysine-stimulated kinase that targets the beta 2-subunit of ap2

Academic Article
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Overview

authors

  • Conner, S. D.
  • Schmid, Sandra

publication date

  • June 2005

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Isolated clathrin adaptor protein (AP) preparations are known to co-fractionate with endogenous kinase activities, including poly-L-lysine-stimulated kinases that target various constituents of the clathrin coat. We have identified CVAK104 (a coated vesicle-associated kinase of 104 kDa) using a mass spectroscopic analysis of adaptor protein preparations. CVAK104 is a novel serine/threonine kinase that belongs to the SCY1-like family of protein kinases, previously thought to be catalytically inactive. We found that CVAK104 co-fractionates with adaptor protein preparations extracted from clathrin-coated vesicles and directly binds to both clathrin and the plasma membrane adaptor, AP2. CVAK104 binds ATP, and kinase assays indicate that it functions in vitro as a poly-L-lysine-stimulated kinase that is capable of autophosphorylation and phosphorylating the beta2-adaptin subunit of AP2.

subject areas

  • Amino Acid Sequence
  • Animals
  • Brain
  • Catalysis
  • Cattle
  • Clathrin
  • Cloning, Molecular
  • DNA, Complementary
  • DNA-Binding Proteins
  • Electrophoresis, Polyacrylamide Gel
  • Glutathione Transferase
  • Humans
  • Immunoblotting
  • Lysine
  • Molecular Sequence Data
  • Phosphorylation
  • Phosphotransferases
  • Phylogeny
  • Polylysine
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • Proteins
  • Proteomics
  • Subcellular Fractions
  • Transcription Factor AP-2
  • Transcription Factors
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.m5202462200

PubMed ID

  • 15809293
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Additional Document Info

start page

  • 21539

end page

  • 21544

volume

  • 280

issue

  • 22

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