UNIGE document Scientific Article
previous document  unige:8973  next document
add to browser collection

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

Pruitt, W. M.
Karnoub, A. E.
Rakauskas, A. C.
Kurakin, Alexei
Kay, B. K.
Sondek, John
show hidden authors show all authors [1 - 10]
Published in Biochimica et Biophysica Acta. 2003, vol. 1640, no. 1, p. 61-68
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 TransportAnimalsBlood Proteins/chemistry/genetics/ metabolismCarrier Proteins/chemistry/genetics/ metabolismMicePhosphoproteins/chemistry/genetics/ metabolismProtein Isoforms/metabolismProtein Structure, TertiarySignal TransductionCdc42 GTP-Binding Protein/ metabolism
PMID: 12676355
Full text
Article - document accessible for UNIGE members only Limited access to UNIGE
(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 https://archive-ouverte.unige.ch/unige:8973

359 hits

0 download


Deposited on : 2010-07-12

Export document
Format :
Citation style :