Structural basis of syndecan-4 phosphorylation as a molecular switch to regulate signaling.

No abstract is available for this paper.

• Publication year

  2006

• Venue

  Journal of Molecular Biology

• Publication date

  2006-01-27

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/J.JMB.2005.09.087PMID 16310216
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Direct binding of syndecan-4 cytoplasmic domain to the catalytic domain of protein kinase C alpha (PKC alpha) increases focal adhesion localization of PKC alpha.

  2003cited by this paper
• Direct Binding of Syndecan-4 Cytoplasmic Domain to the Catalytic Domain of Protein Kinase Cα (PKCα) Increases Focal Adhesion Localization of PKCα*

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• Regulation of Inositol Phospholipid Binding and Signaling through Syndecan-4*

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• Syntenin-Syndecan Binding Requires Syndecan-Synteny and the Co-operation of Both PDZ Domains of Syntenin*

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• Syndecan-4 Deficiency Impairs Focal Adhesion Formation Only under Restricted Conditions*

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• Syndecan-4 Proteoglycan Cytoplasmic Domain and Phosphatidylinositol 4,5-Bisphosphate Coordinately Regulate Protein Kinase C Activity*

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• Regulation of Syndecan-4 Phosphorylation in Vivo *

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• Syndecan-4 Proteoglycan Regulates the Distribution and Activity of Protein Kinase C*

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