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Scientific article
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Role of the pleckstrin homology domain in intersectin-L Dbl homology domain activation of Cdc42 and signaling

Published inBiochimica et biophysica acta, vol. 1640, no. 1, p. 61-68
Publication date2003
Abstract

Intersectin-long (ITSN-L) contains the invariant Dbl homology (DH) and pleckstrin homology (PH) domain structure characteristic of the majority of Dbl family proteins. This strict domain topography suggests that the PH domain serves an essential, conserved function in the regulation of the intrinsic guanine nucleotide exchange activity of the DH domain. We evaluated the role of the PH domain in regulating the DH domain function of ITSN-L. Surprisingly, we found that the PH domain was dispensable for guanine nucleotide exchange activity on Cdc42 in vitro, yet the PH domain enhanced the ability of the DH domain to activate Cdc42 signaling in vivo. PH domains can interact with phosphoinositide substrates and products of phosphatidylinositol 3-kinase (PI3K). However, PI3K activation did not modulate ITSN-L DH domain function in vivo.

Keywords
  • Adaptor Proteins, Vesicular Transport
  • Animals
  • Blood Proteins/chemistry/genetics/ metabolism
  • Carrier Proteins/chemistry/genetics/ metabolism
  • Mice
  • Phosphoproteins/chemistry/genetics/ metabolism
  • Protein Isoforms/metabolism
  • Protein Structure, Tertiary
  • Signal Transduction
  • Cdc42 GTP-Binding Protein/ metabolism
Citation (ISO format)
PRUITT, W. M. et al. Role of the pleckstrin homology domain in intersectin-L Dbl homology domain activation of Cdc42 and signaling. In: Biochimica et biophysica acta, 2003, vol. 1640, n° 1, p. 61–68. doi: 10.1016/s0167-4889(03)00002-8
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ISSN of the journal0006-3002
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