Modulation of Src Homology 3 Proteins by the Proline-Rich Adaptor Protein Shb

1997 ◽  
Vol 231 (2) ◽  
pp. 269-275 ◽  
Author(s):  
Torbjörn Karlsson ◽  
Michael Welsh
Keyword(s):  
Adaptor Protein ◽  
Src Homology 3 ◽  
Src Homology

Interaction of Grb2 SH3 domain with UVRAG in an Alzheimer’s disease–like scenario

2014 ◽  
Vol 92 (3) ◽  
pp. 219-225 ◽  
Author(s):  
Kasturi Roy ◽  
Oishee Chakrabarti ◽  
Debashis Mukhopadhyay
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Growth Factor Receptor ◽  
Adaptor Protein ◽  
Sh3 Domain ◽  
Binding Motifs ◽  
Src Homology 3 ◽  
Src Homology ◽  
Cellular Compartmentalization

Growth factor receptor-bound protein 2 (Grb2) is an adaptor protein which participates in trafficking pathways alongside its role in signaling. Proteins important for actin remodeling and cellular compartmentalization contain SRC Homology 3 (SH3) binding motifs that interact with Grb2. While studying the Grb2–amyloid precursor protein (APP) intracellular domain (AICD) interaction in Alzheimer’s disease cell line models, it was seen that Grb2 colocalized to compartments that mature into autophagosomes. The entrapping of AICD in the Grb2 vesicles and its clearance via autophagosomes was a survival contrivance on the part of the cell. Here, we report that Grb2, when in excess, interacts with ultraviolet radiation resistance-associated gene protein (UVRAG) under excess conditions of AICD–Grb2 or Grb2. The N-terminal SH3 domain of Grb2 specifically interacts with UVRAG, unlike the C-terminal SH3 domain. This interaction helps to understand the role of Grb2 in the autophagic maturation of vesicles.

scholarly journals Intersectin, a Novel Adaptor Protein with Two Eps15 Homology and Five Src Homology 3 Domains

1998 ◽  
Vol 273 (47) ◽  
pp. 31401-31407 ◽  
Author(s):  
Montarop Yamabhai ◽  
Noah G. Hoffman ◽  
Nancy L. Hardison ◽  
Peter S. McPherson ◽  
Luisa Castagnoli ◽  
...  
Keyword(s):  
Adaptor Protein ◽  
Src Homology 3 ◽  
Src Homology

scholarly journals A Novel Src Homology 3 Domain-containing Adaptor Protein, HIP-55, That Interacts with Hematopoietic Progenitor Kinase 1

1999 ◽  
Vol 274 (48) ◽  
pp. 33945-33950 ◽  
Author(s):  
Diana Ensenat ◽  
Zhengbin Yao ◽  
Xuhong Sunny Wang ◽  
Rajashree Kori ◽  
Guisheng Zhou ◽  
...  
Keyword(s):  
Adaptor Protein ◽  
Hematopoietic Progenitor ◽  
Src Homology 3 ◽  
Src Homology 3 Domain ◽  
Src Homology

scholarly journals Molecular and genetic characterization of the interactions between the Drosophila stoned-B protein and DAP-160 (intersectin)

2005 ◽  
Vol 388 (1) ◽  
pp. 195-204 ◽  
Author(s):  
Leonard E. KELLY ◽  
A. Marie PHILLIPS
Keyword(s):  
Synaptic Vesicle ◽  
Stop Codon ◽  
Adaptor Protein ◽  
Binding Motifs ◽  
Reading Frame ◽  
Vesicle Recycling ◽  
Src Homology 3 ◽  
Synaptotagmin I ◽  
Src Homology

The stoned locus of Drosophila produces a dicistronic transcript and encodes two proteins, stoned-A (STNA) and stoned-B (STNB). Both proteins are located at synaptic terminals. The STNB protein contains a domain that has homology with the μ-subunit of the AP (adaptor protein) complex, as well as a number of NPF (Asp-Pro-Phe) motifs known to bind EH (Eps15 homology) domains. Mutations at the stoned locus interact synergistically with mutations at the shibire (dynamin) locus and alter synaptic vesicle endocytosis. The STNB protein has also been shown to interact with synaptic vesicles via synaptogamin-I. We initiated an investigation of the possible interaction of DAP-160 (dynamin-associated protein of 160 kDa), a Drosophila member of the intersectin family, with the STNB protein. We show here that both of the viable stoned alleles interacted with a genetic construct that reduces DAP-160 levels to 25% of normal. One of these stoned alleles contains a substitution resulting in a stop codon in the open reading frame encoding STNB. This allele also shows markedly reduced levels of both DAP-160 and dynamin. As anticipated, the NPF motifs in STNB are found to be high-affinity binding motifs for the EH domains of DAP-160. One of the SH3 (Src homology 3) domains of DAP-160 also interacts with STNB. Finally, we show that immunoprecipitation of STNB from fly head extracts co-precipitates with DAP-160, and we conclude that the interaction of the STNB protein with both synaptotagmin I and DAP-160 may regulate synaptic vesicle recycling by recruiting dynamin to a pre-fission complex.

scholarly journals A novel Src homology 3 domain-containing adaptor protein, HIP-55, that interacts with hematopoietic progenitor kinase 1.

2000 ◽  
Vol 275 (18) ◽  
pp. 14004
Author(s):  
Diana Ensenat ◽  
Zhengbin Yao ◽  
Xuhong Sunny Wang ◽  
Rajashree Kori ◽  
Guisheng Zhou ◽  
...  
Keyword(s):  
Adaptor Protein ◽  
Hematopoietic Progenitor ◽  
Src Homology 3 ◽  
Src Homology 3 Domain ◽  
Src Homology

Interaction of amphiphysins with AP-1 clathrin adaptors at the membrane

2013 ◽  
Vol 450 (1) ◽  
pp. 73-83 ◽  
Author(s):  
Sonja Huser ◽  
Gregor Suri ◽  
Pascal Crottet ◽  
Martin Spiess
Keyword(s):  
Plasma Membrane ◽  
Brefeldin A ◽  
Adaptor Protein ◽  
Trans Golgi Network ◽  
Src Homology 3 ◽  
Amphiphysin 1 ◽  
Src Homology ◽  
Golgi Network

The assembly of clathrin/AP (adaptor protein)-1-coated vesicles on the trans-Golgi network and endosomes is much less studied than that of clathrin/AP-2 vesicles at the plasma membrane for endocytosis. In vitro, the association of AP-1 with protein-free liposomes had been shown to require phosphoinositides, Arf1 (ADP-ribosylation factor 1)–GTP and additional cytosolic factor(s). We have purified an active fraction from brain cytosol and found it to contain amphiphysin 1 and 2 and endophilin A1, three proteins known to be involved in the formation of AP-2/clathrin coats at the plasma membrane. Assays with bacterially expressed and purified proteins showed that AP-1 stabilization on liposomes depends on amphiphysin 2 or the amphiphysin 1/2 heterodimer. Activity is independent of the SH3 (Src homology 3) domain, but requires interaction of the WDLW motif with γ-adaptin. Endogenous amphiphysin in neurons and transfected protein in cell lines co-localize perinuclearly with AP-1 at the trans-Golgi network. This localization depends on interaction of clathrin and the adaptor sequence in the amphiphysins and is sensitive to brefeldin A, which inhibits Arf1-dependent AP-1 recruitment. Interaction between AP-1 and amphiphysin 1/2 in vivo was demonstrated by co-immunoprecipitation after cross-linking. These results suggest an involvement of amphiphysins not only with AP-2 at the plasma membrane, but also in AP-1/clathrin coat formation at the trans-Golgi network.

scholarly journals An Adaptor Role for Cytoplasmic Sam68 in Modulating Src Activity during Cell Polarization

2009 ◽  
Vol 29 (7) ◽  
pp. 1933-1943 ◽  
Author(s):  
Marc-Étienne Huot ◽  
Claire M. Brown ◽  
Nathalie Lamarche-Vane ◽  
Stéphane Richard
Keyword(s):  
Plasma Membrane ◽  
Rho Gtpases ◽  
Cell Attachment ◽  
Adaptor Protein ◽  
Cell Polarization ◽  
Sh2 Domains ◽  
Src Homology 3 ◽  
Rac1 Activity ◽  
Small Rho Gtpases ◽  
Src Homology

ABSTRACT The Src-associated substrate during mitosis with a molecular mass of 68 kDa (Sam68) is predominantly nuclear and is known to associate with proteins containing the Src homology 3 (SH3) and SH2 domains. Although Sam68 is a Src substrate, little is known about the signaling pathway that link them. Src is known to be activated transiently after cell spreading, where it modulates the activity of small Rho GTPases. Herein we report that Sam68-deficient cells exhibit loss of cell polarity and cell migration. Interestingly, Sam68-deficient cells exhibited sustained Src activity after cell attachment, resulting in the constitutive tyrosine phosphorylation and activation of p190RhoGAP and its association with p120rasGAP. Consistently, we observed that Sam68-deficient cells exhibited deregulated RhoA and Rac1 activity. By using total internal reflection fluorescence microscopy, we observed Sam68 near the plasma membrane after cell attachment coinciding with phosphorylation of its C-terminal tyrosines and association with Csk. These findings show that Sam68 localizes near the plasma membrane during cell attachment and serves as an adaptor protein to modulate Src activity for proper signaling to small Rho GTPases.

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