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Signal transducing adaptor molecule

This gene encodes a member of the signal-transducing adaptor molecule family. These proteins mediate downstream signaling of cytokine receptors and also play a role in ER to Golgi trafficking by interacting with the coat protein II complex. The encoded protein also associates with hepatocyte growth factor-regulated substrate to form the endosomal sorting complex required for transport-0 (ESCRT-0), which sorts ubiquitinated membrane proteins to the ESCRT-1 complex for lysosomal degradation. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, Feb 2011] (from NCBI)
Top mentioned proteins: HRs, Ubiquitin, STAM2, V1a, CAN
Papers on Stam
Rme-8 depletion perturbs Notch recycling and predisposes to pathogenic signaling.
Bray et al., Düsseldorf, Germany. In J Cell Biol, Aug 2015
Likewise, depletion of ESCRT-0 components Hrs or Stam in combination with Rme-8 also led to high levels of ectopic Notch activity.
An SH3 binding motif within the nucleocapsid protein of porcine reproductive and respiratory syndrome virus interacts with the host cellular signaling proteins STAMI, TXK, Fyn, Hck, and cortactin.
Meng et al., Blacksburg, United States. In Virus Res, Jul 2015
Subsequently, we identified five host cellular proteins [signal transducing adaptor molecule (STAM)I, TXK tyrosine kinase (TXK), protein tyrosine kinase fyn (Fyn), hematopoietic cell kinase (Hck), and cortactin] that interact with this SH3 motif.
ESCRT-0 protein hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) is targeted to endosomes independently of signal-transducing adaptor molecule (STAM) and the complex formation with STAM promotes its endosomal dissociation.
Takeshita et al., Matsumoto, Japan. In J Biol Chem, 2014
In this study, we have found that co-expressing exogenous STAM1 in Hrs-overexpressing cells leads to a diffuse localization for a large part of the Hrs accumulated on endosomes and a recovery of the impaired cargo protein degradation process, thus suggesting that exogenous STAM abrogates the abnormalities of the Hrs-positive endosomes.
Lgl regulates Notch signaling via endocytosis, independently of the apical aPKC-Par6-Baz polarity complex.
Richardson et al., Melbourne, Australia. In Curr Biol, 2014
Upregulation of Notch signaling in lgl- tissue requires dynamin- and Rab5-mediated endocytosis and vesicle acidification but is independent of Hrs/Stam or Rab11 activity.
Analysis of ESCRT functions in exosome biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles.
Raposo et al., Paris, France. In J Cell Sci, 2014
Silencing of HRS, STAM1 or TSG101 reduced the secretion of EV-associated CD63 and MHC II but each gene altered differently the size and/or protein composition of secreted EVs, as quantified by immuno-electron microscopy.
Proteomic investigation of the hippocampus in prenatally stressed mice implicates changes in membrane trafficking, cytoskeletal, and metabolic function.
Cotter et al., Dublin, Ireland. In Dev Neurosci, 2013
Western blotting was utilized to validate the changes in calretinin, hippocalcin, profilin-1 and the signal-transducing adaptor molecule STAM1.
ESCRT-0 is not required for ectopic Notch activation and tumor suppression in Drosophila.
Vaccari et al., Milano, Italy. In Plos One, 2013
Here, we report that two Drosophila epithelia lacking activity of Stam, the other known components of the ESCRT-0 complex, or of both Hrs and Stam, accumulate the signaling receptors Notch and Dome in endosomes.
Factors related to the use of reperfusion strategies in elderly patients with acute myocardial infarction.
Wang et al., Beijing, China. In J Cardiothorac Surg, 2013
METHODS: A total of 352 consecutive elderly patients (≥65 years) with ST-elevated AMI (STAMI) were admitted, they were divided into 2 groups based on reperfusion treatment (thrombolysis or percutaneous coronary intervention, PCI): reperfusion therapy group (n = 268) and non-reperfusion therapy group (n = 84).
Direct binding of the Kex2p cytosolic tail to the VHS domain of yeast Gga2p facilitates TGN to prevacuolar compartment transport and is regulated by phosphorylation.
Fuller et al., Ann Arbor, United States. In Mol Biol Cell, 2013
Two-hybrid analysis shows that the Gga1p and Gga2p Vps27, Hrs, Stam (VHS) domains both bind a site in the Kex2p C-tail and that the Gga2p VHS domain binds a site in the Vps10p C-tail.
Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the ESCRT machinery in endosomal trafficking.
Li et al., Atlanta, United States. In J Cell Biol, 2012
Here, we report that SIMPLE interacted and colocalized with endosomal sorting complex required for transport (ESCRT) components STAM1, Hrs, and TSG101 on early endosomes and functioned with the ESCRT machinery in the control of endosome-to-lysosome trafficking.
Evidence for cooperative and domain-specific binding of the signal transducing adaptor molecule 2 (STAM2) to Lys63-linked diubiquitin.
Walker et al., Villeurbanne, France. In J Biol Chem, 2012
ESCRT-0 is formed by two subunits known as Hrs (hepatocyte growth factor-regulated substrate) and STAM (signal transducing adaptor molecule), both of which harbor multiple ubiquitin-binding domains (UBDs).
Novel roles for the E3 ubiquitin ligase atrophin-interacting protein 4 and signal transduction adaptor molecule 1 in G protein-coupled receptor signaling.
Marchese et al., Maywood, United States. In J Biol Chem, 2012
Overexpression of an AIP4 catalytically inactive mutant and a mutant that shows poor binding to STAM-1 fails to enhance CXCR4-induced ERK-1/2 signaling.
Backbone 1H, 13C, and 15N assignments for the tandem ubiquitin binding domains of signal transducing adapter molecule 1.
Ahn et al., Seoul, South Korea. In Biomol Nmr Assign, 2011
Signal transducing adapter molecule (STAM) forms the endosomal sorting complex required for transport-0 (ESCRT-0) complex with hepatocyte growth factor-regulated substrate (Hrs) to sort the ubiquitinated cargo proteins from the early endosomes to the ESCRT-1 complex.
Solution structure of UIM and interaction of tandem ubiquitin binding domains in STAM1 with ubiquitin.
Ahn et al., Taejŏn, South Korea. In Biochem Biophys Res Commun, 2011
STAM1 and Hrs are the components of ESCRT-0 complex for lysosomal degradation of membrane proteins is composed of STAM1 Hrs and has multiple ubiquitin binding domains.
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Walker et al., Villeurbanne, France. In Biochemistry, 2011
Among all VHS domains, the VHS domain of Stam proteins is the strongest binder to monoubiqiuitin and exhibits preferences for K63-linked chains.
STAM adaptor proteins interact with COPII complexes and function in ER-to-Golgi trafficking.
Blackstone et al., Bethesda, United States. In Traffic, 2009
STAMs function prominently in endoplasmic reticulum-to-Golgi trafficking, most likely through direct interactions with the coat protein II complex
Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy.
Lee et al., Seoul, South Korea. In Febs Lett, 2009
A novel ubiquitin binding site and the manner of ubiquitin recognition of the STAM1 VHS domain were proposed.
The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation.
Urbé et al., Liverpool, United Kingdom. In J Biol Chem, 2006
The cellular functions of UBPY are complex but clearly distinct from those of the Lys-63-ubiquitin-specific protease, AMSH, with which it shares a binding site on the SH3 domain of STAM
Growth factors induce differential phosphorylation profiles of the Hrs-STAM complex: a common node in signalling networks with signal-specific properties.
Urbé et al., Liverpool, United Kingdom. In Biochem J, 2005
Analysis with phospho-specific antibodies indicates that 3 kinases generate a signal-specific, combinatorial phosphorylation profile of the Hrs-STAM complex, with the potential of diversifying tyrosine kinase receptor signalling through a common element.
Structural and mechanistic aspects of Janus kinases: how the two-faced god wields a double-edged sword.
Farrar et al., Frederick, United States. In J Interferon Cytokine Res, 1998
A fourth domain determining substrate specificity is as yet poorly defined and is, therefore, discussed in the context of known substrates and inhibitors, a collection of molecules that have been expanded recently to include Stam and Jab.
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