scholarly journals Molecular basis of interactions between SH3 domain-containing proteins and the proline-rich region of the ubiquitin ligase Itch

2017 ◽  
Vol 292 (15) ◽  
pp. 6325-6338 ◽  
Author(s):  
Guillaume Desrochers ◽  
Laurent Cappadocia ◽  
Mathieu Lussier-Price ◽  
Anh-Tien Ton ◽  
Riham Ayoubi ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Molecular Basis ◽  
Sh3 Domain ◽  
Rich Region ◽  
Proline Rich Region

scholarly journals Identification of a Phospholipase C-γ1 (PLC-γ1) SH3 Domain-Binding Site in SLP-76 Required for T-Cell Receptor-Mediated Activation of PLC-γ1 and NFAT

2001 ◽  
Vol 21 (13) ◽  
pp. 4208-4218 ◽  
Author(s):  
Deborah Yablonski ◽  
Theresa Kadlecek ◽  
Arthur Weiss
Keyword(s):  
T Cell ◽  
Phospholipase C ◽  
T Cell Receptor ◽  
Function Analysis ◽  
Cell Receptor ◽  
Sh3 Domain ◽  
Functional Domain ◽  
Rich Region ◽  
Activated T Cells ◽  
Proline Rich Region

ABSTRACT SLP-76 is an adapter protein required for T-cell receptor (TCR) signaling. In particular, TCR-induced tyrosine phosphorylation and activation of phospholipase C-γ1 (PLC-γ1), and the resultant TCR-inducible gene expression, depend on SLP-76. Nonetheless, the mechanisms by which SLP-76 mediates PLC-γ1 activation are not well understood. We now demonstrate that SLP-76 directly interacts with the Src homology 3 (SH3) domain of PLC-γ1. Structure-function analysis of SLP-76 revealed that each of the previously defined protein-protein interaction domains can be individually deleted without completely disrupting SLP-76 function. Additional deletion mutations revealed a new, 67-amino-acid functional domain within the proline-rich region of SLP-76, which we have termed the P-1 domain. The P-1 domain mediates a constitutive interaction of SLP-76 with the SH3 domain of PLC-γ1 and is required for TCR-mediated activation of Erk, PLC-γ1, and NFAT (nuclear factor of activated T cells). The adjacent Gads-binding domain of SLP-76, also within the proline-rich region, mediates inducible recruitment of SLP-76 to a PLC-γ1-containing complex via the recruitment of both PLC-γ1 and Gads to another cell-type-specific adapter, LAT. Thus, TCR-induced activation of PLC-γ1 entails the binding of PLC-γ1 to both LAT and SLP-76, a finding that may underlie the requirement for both LAT and SLP-76 to mediate the optimal activation of PLC-γ1.

scholarly journals The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro

2014 ◽  
Vol 34 (6) ◽  
Author(s):  
Miguel De Avila ◽  
Kenrick A. Vassall ◽  
Graham S. T. Smith ◽  
Vladimir V. Bamm ◽  
George Harauz
Keyword(s):  
Tyrosine Kinase ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Sh3 Domain ◽  
Rich Region ◽  
Fyn Kinase ◽  
Oligodendrocyte Development ◽  
In Vitro Interaction ◽  
Proline Rich Region

MBP interacts with Fyn kinase during oligodendrocyte development and myelination. We show that there is no binding-induced PPII formation in the primary ligand segment, and that a region upstream is required for in vitro interaction.

scholarly journals The SH3 domain of a M7 interacts with its C-terminal proline-rich region

2007 ◽  
Vol 16 (2) ◽  
pp. 189-196 ◽  
Author(s):  
Qinghua Wang ◽  
Matthew A. Deloia ◽  
Yang Kang ◽  
Casey Litchke ◽  
Naixia Zhang ◽  
...  
Keyword(s):  
Sh3 Domain ◽  
Rich Region ◽  
Proline Rich Region

scholarly journals Correction to Multiple Src Homology 3 Binding to the Ubiquitin Ligase Itch Conserved Proline-Rich Region

Biochemistry ◽  
2016 ◽  
Vol 55 (22) ◽  
pp. 3174-3174
Author(s):  
Guillaume Desrochers ◽  
Mathieu Lussier-Price ◽  
James G. Omichinski ◽  
Annie Angers
Keyword(s):  
Ubiquitin Ligase ◽  
Rich Region ◽  
Src Homology 3 ◽  
Src Homology ◽  
Proline Rich Region

scholarly journals A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization.

1996 ◽  
Vol 16 (2) ◽  
pp. 548-556 ◽  
Author(s):  
N L Freeman ◽  
T Lila ◽  
K A Mintzer ◽  
Z Chen ◽  
A J Pahk ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Adenylyl Cyclase ◽  
Sh3 Domain ◽  
Regulatory Function ◽  
Nucleotide Exchange ◽  
Cortical Actin ◽  
Rich Region ◽  
Sh3 Domains ◽  
Proline Rich Region

Saccharomyces cerevisiae cyclase-associated protein (CAP or Srv2p) is multifunctional. The N-terminal third of CAP binds to adenylyl cyclase and has been implicated in adenylyl cyclase activation in vivo. The widely conserved C-terminal domain of CAP binds to monomeric actin and serves an important cytoskeletal regulatory function in vivo. In addition, all CAP homologs contain a centrally located proline-rich region which has no previously identified function. Recently, SH3 (Src homology 3) domains were shown to bind to proline-rich regions of proteins. Here we report that the proline-rich region of CAP is recognized by the SH3 domains of several proteins, including the yeast actin-associated protein Abp1p. Immunolocalization experiments demonstrate that CAP colocalizes with cortical actin-containing structures in vivo and that a region of CAP containing the SH3 domain binding site is required for this localization. We also demonstrate that the SH3 domain of yeast Abp1p and that of the yeast RAS protein guanine nucleotide exchange factor Cdc25p complex with adenylyl cyclase in vitro. Interestingly, the binding of the Cdc25p SH3 domain is not mediated by CAP and therefore may involve direct binding to adenylyl cyclase or to an unidentified protein which complexes with adenylyl cyclase. We also found that CAP homologous from Schizosaccharomyces pombe and humans bind SH3 domains. The human protein binds most strongly to the SH3 domain from the abl proto-oncogene. These observations identify CAP as an SH3 domain-binding protein and suggest that CAP mediates interactions between SH3 domain proteins and monomeric actin.

scholarly journals Determinants of High Titer in Recombinant Porcine Endogenous Retroviruses

2004 ◽  
Vol 78 (24) ◽  
pp. 13871-13879 ◽  
Author(s):  
Ian Harrison ◽  
Yasuhiro Takeuchi ◽  
Birke Bartosch ◽  
Jonathan P. Stoye
Keyword(s):  
Molecular Basis ◽  
High Titer ◽  
Human Cells ◽  
Endogenous Retroviruses ◽  
The Novel ◽  
Rich Region ◽  
Variable Regions ◽  
Porcine Endogenous Retroviruses ◽  
Primary Determinant ◽  
Proline Rich Region

ABSTRACT Porcine endogenous retroviruses (PERVs) pose a potential stumbling block for therapeutic xenotransplantation, with the greatest threat coming from viruses generated by recombination between members of the PERV subgroup A (PERV-A) and PERV-C families (PERV-A/C recombinants). PERV-A and PERV-B have been shown to infect human cells in culture, albeit with low titers. PERV-C has a more restricted host range and cannot infect human cells. A recombinant PERV-A/C virus (PERV-A14/220) contains the PERV-A sequence between the end of pol and the middle of the SU region in env. The remaining sequence is derived from PERV-C. PERV-A14/220 is approximately 500-fold more infectious than PERV-A. To determine the molecular basis for the increased infectivity of PERV-A14/220, we have made a series of vector constructs. The primary determinant for the enhanced replicative potential of the recombinant virus appeared to be the env gene. Using a series of chimeric env genes, we could identify two determinants of high infectivity; one was an isoleucine to valine substitution at position 140 between variable regions A and B, and the other lies within the proline rich region. Taken together, these results show that the novel juxtaposition of env gene sequences enhanced the infectivity of PERV-A14/220 for human cells, perhaps by stabilization of the envelope glycoprotein or increased receptor binding.

scholarly journals Multiple Src Homology 3 Binding to the Ubiquitin Ligase Itch Conserved Proline-Rich Region

Biochemistry ◽  
2015 ◽  
Vol 54 (50) ◽  
pp. 7345-7354 ◽  
Author(s):  
Guillaume Desrochers ◽  
Mathieu Lussier-Price ◽  
James G. Omichinski ◽  
Annie Angers
Keyword(s):  
Ubiquitin Ligase ◽  
Rich Region ◽  
Src Homology 3 ◽  
Src Homology ◽  
Proline Rich Region
Sign in / Sign up

Export Citation Format

Share Document