Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP
@article{Hussain2001EndocyticPI, title={Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP}, author={Natasha K. Hussain and Sarah Jenna and Michael Glogauer and Christopher C. Quinn and Sylwia Wasiak and Michel Guipponi and Stylianos E. Antonarakis and Brian K. Kay and Thomas Peter Stossel and Nathalie Lamarche-Vane and Peter S. McPherson}, journal={Nature Cell Biology}, year={2001}, volume={3}, pages={927-932} }
Intersectin-s is a modular scaffolding protein regulating the formation of clathrin-coated vesicles. In addition to the Eps15 homology (EH) and Src homology 3 (SH3) domains of intersectin-s, the neuronal variant (intersectin-l) also has Dbl homology (DH), pleckstrin homology (PH) and C2 domains. We now show that intersectin-l functions through its DH domain as a guanine nucleotide exchange factor (GEF) for Cdc42. In cultured cells, expression of DH-domain-containing constructs cause actin…
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References
SHOWING 1-10 OF 39 REFERENCES
Splice Variants of Intersectin Are Components of the Endocytic Machinery in Neurons and Nonneuronal Cells*
- BiologyThe Journal of Biological Chemistry
- 1999
Immunofluorescence analysis of cultured hippocampal neurons and antibodies against intersectin co-immunoprecipitate clathrin, AP2, and dynamin from brain extracts suggest that the long and short forms of intersectin are components of the endocytic machinery in neurons and nonneuronal cells.
Intersectin 2, a new multimodular protein involved in clathrin‐mediated endocytosis
- BiologyFEBS letters
- 2000
CdGAP, a Novel Proline-rich GTPase-activating Protein for Cdc42 and Rac*
- BiologyThe Journal of Biological Chemistry
- 1998
A novel serine- and proline-rich GTPase-activating protein, CdGAP, which is active in vitro on both Cdc42 and Rac and likely to participate in CDC42- and Rac-induced signaling pathways leading to actin reorganization is identified.
Yeast Eps15-like endocytic protein, Pan1p, activates the Arp2/3 complex
- BiologyNature Cell Biology
- 2001
It is suggested that Pan1p forms the core of an endocytic complex and physically couples actin polymerization nucleated by the Arp2/3 complex to the endocytical machinery, thus providing the forces necessary for endocytosis.
N‐WASP, a novel actin‐depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2‐dependent manner downstream of tyrosine kinases.
- BiologyThe EMBO journal
- 1996
It is concluded that N‐WASP transmits signals from tyrosine kinases to cause a polarized rearrangement of cortical actin filaments dependent on PIP2.
The endocytic protein intersectin is a major binding partner for the Ras exchange factor mSos1 in rat brain
- BiologyThe EMBO journal
- 2000
The discovery of a brain‐enriched, 170 kDa protein that interacts specifically with SH3A suggests that intersectin functions in cell signaling in addition to its role in endocytosis and may link these cellular processes.
Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP
- BiologyNature
- 1998
It is demonstrated that before it can induce filopodium formation, Cdc42 must bind a WASP-related protein, N-WASP, that is richest in neural tissues but is expressed ubiquitously.
Two Pathways through Cdc42 Couple the N-Formyl Receptor to Actin Nucleation in Permeabilized Human Neutrophils
- BiologyThe Journal of cell biology
- 2000
A permeabilization method that retains coupling between N-formyl-methionyl-leucyl-phenylalanine tripeptide (FMLP) receptor stimulation, shape changes, and barbed-end actin nucleation in human neutrophils is developed and concludes that this alternate involves phosphoinositide-mediated uncapping of actin filament barbed ends.
SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation
- Biology, ChemistryNature Cell Biology
- 1999
The efficient reconstitution of ATP-, GTP-, cytosol- and dynamin-dependent formation of clathrin-coated vesicles in permeabilized 3T3-L1 cells is reported, suggesting that interactions between SH3 domains and their partners function sequentially in endocytic coated-vesicle formation.
EPS8 and E3B1 transduce signals from Ras to Rac
- Biology, ChemistryNature
- 1999
It is shown that Eps8 and E3b1/Abi-1 participate in the transduction of signals from Ras to Rac, by regulating Rac-specific guanine nucleotide exchange factor (GEF) activities.