Overexpression of p97Eps8 leads to cellular transformation: implication of pleckstrin homology domain in p97Eps8-mediated ERK activation

No abstract is available for this paper.

• Publication year

  2001

• Venue

  Oncogene

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1038/sj.onc.1204069PMID 11244499
• 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.

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  2000cited by this paper
• A novel peptide–SH3 interaction

  1999cited by this paper
• Enhancement of tyrosyl phosphorylation and protein expression of eps8 by v-Src.

  1999cited by this paper
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  1999influential reference
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  1998cited by this paper
• Activation of phospholipase Cγ by PI 3‐kinase‐induced PH domain‐mediated membrane targeting

  1998cited by this paper
• Eps8, a tyrosine kinase substrate, is recruited to the cell cortex and dynamic F-actin upon cytoskeleton remodeling.

  1998cited by this paper
• Specificity and Promiscuity in Phosphoinositide Binding by Pleckstrin Homology Domains*

  1998cited by this paper
• Signaling through scaffold, anchoring, and adaptor proteins.

  1997cited by this paper
• A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain

  1997cited by this paper
• High Affinity Binding of Inositol Phosphates and Phosphoinositides to the Pleckstrin Homology Domain of RAC/Protein Kinase B and Their Influence on Kinase Activity*

  1997cited by this paper
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  1997cited by this paper
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  1997cited by this paper
• Regulation of the tyrosine kinase substrate Eps8 expression by growth factors, v-Src and terminal differentiation

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• The SH3 domain of Eps8 exists as a novel intertwined dimer

  1997cited by this paper
• Immune complex kinase assays for mitogen-activated protein kinase and MEK.

  1995cited by this paper
• Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain.

  1995cited by this paper
• Constitutive phosphorylation of eps8 in tumor cell lines: relevance to malignant transformation

  1995cited by this paper
• Binding of beta gamma subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase.

  1994cited by this paper
• Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate

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• Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF‐dependent mitogenic signals.

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• The PH domain: a common piece in the structural patchwork of signalling proteins.

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  2014cites this paper
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  2014cites this paper
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  2010cites this paper
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  2010cites this paper
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  2009cites this paper
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• EPS8 Facilitates Cellular Growth and Motility of Colon Cancer Cells by Increasing the Expression and Activity of Focal Adhesion Kinase*

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