Structure and ligand recognition of the phosphotyrosine binding domain of Shc

Nature ◽  
1995 ◽  
Vol 378 (6557) ◽  
pp. 584-592 ◽  
Author(s):  
Ming-Ming Zhou ◽  
Kodimangalam S. Ravichandran ◽  
Edward T. Olejniczak ◽  
Andrew M. Petros ◽  
Robert P. Meadows ◽  
...  
Keyword(s):  
Binding Domain ◽  
Ligand Recognition ◽  
Phosphotyrosine Binding Domain

A Folded Excited State of Ligand-Free Nuclear Coactivator Binding Domain (NCBD) Underlies Plasticity in Ligand Recognition

Biochemistry ◽  
2013 ◽  
Vol 52 (10) ◽  
pp. 1686-1693 ◽  
Author(s):  
Magnus Kjaergaard ◽  
Lisbeth Andersen ◽  
Lau Dalby Nielsen ◽  
Kaare Teilum
Keyword(s):  
Excited State ◽  
Binding Domain ◽  
Ligand Recognition ◽  
Ligand Free

scholarly journals Serine Phosphorylation Proximal to Its Phosphotyrosine Binding Domain Inhibits Insulin Receptor Substrate 1 Function and Promotes Insulin Resistance

2004 ◽  
Vol 24 (21) ◽  
pp. 9668-9681 ◽  
Author(s):  
Yan-Fang Liu ◽  
Avia Herschkovitz ◽  
Sigalit Boura-Halfon ◽  
Denise Ronen ◽  
Keren Paz ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Insulin Receptor ◽  
Insulin Signaling ◽  
Insulin Treatment ◽  
Binding Domain ◽  
Serine Phosphorylation ◽  
Insulin Receptor Substrate ◽  
Control Mechanisms ◽  
Insulin Receptor Substrate 1 ◽  
Phosphotyrosine Binding Domain

ABSTRACT Ser/Thr phosphorylation of insulin receptor substrate (IRS) proteins negatively modulates insulin signaling. Therefore, the identification of serine sites whose phosphorylation inhibit IRS protein functions is of physiological importance. Here we mutated seven Ser sites located proximal to the phosphotyrosine binding domain of insulin receptor substrate 1 (IRS-1) (S265, S302, S325, S336, S358, S407, and S408) into Ala. When overexpressed in rat hepatoma Fao or CHO cells, the mutated IRS-1 protein in which the seven Ser sites were mutated to Ala (IRS-17A), unlike wild-type IRS-1 (IRS-1WT), maintained its Tyr-phosphorylated active conformation after prolonged insulin treatment or when the cells were challenged with inducers of insulin resistance prior to acute insulin treatment. This was due to the ability of IRS-17A to remain complexed with the insulin receptor (IR), unlike IRS-1WT, which underwent Ser phosphorylation, resulting in its dissociation from IR. Studies of truncated forms of IRS-1 revealed that the region between amino acids 365 to 430 is a main insulin-stimulated Ser phosphorylation domain. Indeed, IRS-1 mutated only at S408, which undergoes phosphorylation in vivo, partially maintained the properties of IRS-17A and conferred protection against selected inducers of insulin resistance. These findings suggest that S408 and additional Ser sites among the seven mutated Ser sites are targets for IRS-1 kinases that play a key negative regulatory role in IRS-1 function and insulin action. These sites presumably serve as points of convergence, where physiological feedback control mechanisms, which are triggered by insulin-stimulated IRS kinases, overlap with IRS kinases triggered by inducers of insulin resistance to terminate insulin signaling.

scholarly journals Characterization of the Phosphotyrosine-binding Domain of theDrosophilaShc Protein

1996 ◽  
Vol 271 (50) ◽  
pp. 31855-31862 ◽  
Author(s):  
Shun-Cheng Li ◽  
Ka-Man Venus Lai ◽  
Gerald D. Gish ◽  
Wendy E. Parris ◽  
Peter van der Geer ◽  
...  
Keyword(s):  
Binding Domain ◽  
Phosphotyrosine Binding Domain

scholarly journals Structural Basis for the Specific Recognition of RET by the Dok1 Phosphotyrosine Binding Domain

2003 ◽  
Vol 279 (6) ◽  
pp. 4962-4969 ◽  
Author(s):  
Ning Shi ◽  
Sheng Ye ◽  
Mark Bartlam ◽  
Maojun Yang ◽  
Jing Wu ◽  
...  
Keyword(s):  
Binding Domain ◽  
Structural Basis ◽  
Specific Recognition ◽  
Phosphotyrosine Binding Domain

scholarly journals RET PLCγ Phosphotyrosine Binding Domain Regulates Ca2+ Signaling and Neocortical Neuronal Migration

PLoS ONE ◽  
2012 ◽  
Vol 7 (2) ◽  
pp. e31258 ◽  
Author(s):  
T. Kalle Lundgren ◽  
Katsutoshi Nakahata ◽  
Nicolas Fritz ◽  
Paola Rebellato ◽  
Songbai Zhang ◽  
...  
Keyword(s):  
Neuronal Migration ◽  
Binding Domain ◽  
Phosphotyrosine Binding Domain

scholarly journals Mutations in a Gene Encoding a Novel Protein Containing a Phosphotyrosine-Binding Domain Cause Type 2 Cerebral Cavernous Malformations

2003 ◽  
Vol 73 (6) ◽  
pp. 1459-1464 ◽  
Author(s):  
Christina L. Liquori ◽  
Michel J. Berg ◽  
Adrian M. Siegel ◽  
Elizabeth Huang ◽  
Jon S. Zawistowski ◽  
...  
Keyword(s):  
Binding Domain ◽  
Cerebral Cavernous Malformations ◽  
Gene Encoding ◽  
Cavernous Malformations ◽  
Phosphotyrosine Binding Domain ◽  
Novel Protein

scholarly journals Interaction of the Akt Substrate, AS160, with the Glucose Transporter 4 Vesicle Marker Protein, Insulin-Regulated Aminopeptidase

2006 ◽  
Vol 20 (10) ◽  
pp. 2576-2583 ◽  
Author(s):  
Grantley R. Peck ◽  
Siying Ye ◽  
Vi Pham ◽  
Ruani N. Fernando ◽  
S. Lance Macaulay ◽  
...  
Keyword(s):  
Glucose Transporter ◽  
Binding Domain ◽  
Amino Terminus ◽  
Glucose Transporter 4 ◽  
Marker Protein ◽  
Intracellular Pool ◽  
Storage Vesicles ◽  
Endogenous Proteins ◽  
Endosomal System ◽  
Phosphotyrosine Binding Domain

Abstract Insulin-regulated aminopeptidase (IRAP), a marker of glucose transporter 4 (GLUT4) storage vesicles (GSVs), is the only protein known to traffic with GLUT4. In the basal state, GSVs are sequestered from the constitutively recycling endosomal system to an insulin-responsive, intracellular pool. Insulin induces a rapid translocation of GSVs to the cell surface from this pool, resulting in the incorporation of IRAP and GLUT4 into the plasma membrane. We sought to identify proteins that interact with IRAP to further understand this GSV trafficking process. This study describes our identification of a novel interaction between the amino terminus of IRAP and the Akt substrate, AS160 (Akt substrate of 160 kDa). The validity of this interaction was confirmed by coimmunoprecipitation of both overexpressed and endogenous proteins. Moreover, confocal microscopy demonstrated colocalization of these proteins. In addition, we demonstrate that the IRAP-binding domain of AS160 falls within its second phosphotyrosine-binding domain and the interaction is not regulated by AS160 phosphorylation. We hypothesize that AS160 is localized to GLUT4-containing vesicles via its interaction with IRAP where it inhibits the activity of Rab substrates in its vicinity, effectively tethering the vesicles intracellularly.

scholarly journals Engineering the Recruitment of Phosphotyrosine Binding Domain-containing Adaptor Proteins Reveals Distinct Roles for RET Receptor-mediated Cell Survival

2006 ◽  
Vol 281 (40) ◽  
pp. 29886-29896 ◽  
Author(s):  
T. Kalle Lundgren ◽  
Rizaldy P. Scott ◽  
Matthew Smith ◽  
Tony Pawson ◽  
Patrik Ernfors
Keyword(s):  
Cell Survival ◽  
Adaptor Proteins ◽  
Binding Domain ◽  
Phosphotyrosine Binding Domain
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