hTRPC1-associated alpha-actinin, and not hTRPC1 itself, is tyrosine phosphorylated during human platelet activation

P C Redondo, A G S Harper, M T Harper, S L Brownlow, J A Rosado, S O Sage

Research output: Contribution to journalArticle (Academic Journal)peer-review

6 Citations (Scopus)

Abstract

Canonical transient receptor potential channels (TRPCs), which are regulated by several processes, including tyrosine phosphorylation, are candidates for the conduction of store-operated Ca(2+) entry (SOCE).
Original languageEnglish
Pages (from-to)2476-83
Number of pages8
JournalJournal of Thrombosis and Haemostasis
Volume5
Issue number12
DOIs
Publication statusPublished - Dec 2007

Keywords

  • Thrombin
  • Phosphotyrosine
  • Humans
  • Actinin
  • Immunoprecipitation
  • Tyrosine
  • Protein-Tyrosine Kinases
  • Platelet Activation
  • Enzyme Inhibitors
  • Membrane Proteins
  • Blood Platelets
  • Blotting, Western
  • Neoplasm Proteins
  • Multiprotein Complexes
  • Phosphorylation
  • TRPC Cation Channels
  • Quinolines
  • Time Factors
  • Protein Tyrosine Phosphatase, Non-Receptor Type 6
  • Calcium Signaling

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