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STN1 Stn1p

Stn1, SALF, Stn1p
Endocytosis of cell surface proteins is mediated by a complex molecular machinery that assembles on the inner surface of the plasma membrane. This gene encodes one of two human homologs of the Drosophila melanogaster stoned B protein. This protein is related to components of the endocytic machinery and exhibits a modular structure consisting of an N-terminal proline-rich domain, a central region of homology specific to the human stoned B-like proteins, and a C-terminal region homologous to the mu subunits of adaptor protein (AP) complexes. Read-through transcription of this gene into the neighboring downstream gene, which encodes TFIIA-alpha/beta-like factor, generates a transcript (SALF), which encodes a fusion protein comprised of sequence sharing identity with each individual gene product. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2010] (from NCBI)
Top mentioned proteins: CAN, ACID, POLYMERASE, RPA, Thymopentin
Papers using Stn1 antibodies
Synaptotagmin I is a high affinity receptor for clathrin AP-2implications for membrane recycling
Supplier
Bonifacino Juan S. et al., In The Journal of Cell Biology, 1993
... Primers corresponding to SALF were used in 5′- and 3′-RACE PCR on a Marathon-Ready™ human heart cDNA library (CLONTECH Laboratories, Inc.) to isolate ...
Papers on Stn1
Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.
New
Impact
Feigon et al., Los Angeles, United States. In Science, Nov 2015
The p75-p45-p19 subcomplex is identified as another RPA-related complex, CST (CTC1-STN1-TEN1).
Enhanced Control of Bladder-Associated Tumors Using Shrimp Anti-Lipopolysaccharide Factor (SALF) Antimicrobial Peptide as a Cancer Vaccine Adjuvant in Mice.
New
Wu et al., Chi-lung, Taiwan. In Mar Drugs, May 2015
Shrimp anti-lipopolysaccharide factor (SALF) is an antimicrobial peptide with reported anticancer activities, such as suppression of tumor progression.
Evolution of the Telomere-Associated Protein POT1a in Arabidopsis thaliana Is Characterized by Positive Selection to Reinforce Protein-Protein Interaction.
New
Shippen et al., Kazan', Russia. In Mol Biol Evol, May 2015
In vitro-binding studies demonstrated that all three sites under positive selection specifically enhance the AtPOT1a interaction with CTC1, a core component of the highly conserved CST (CTC1/STN1/TEN1) telomere protein complex.
DNA-Directed Polymerase Subunits Play a Vital Role in Human Telomeric Overhang Processing.
New
Loayza et al., New York City, United States. In Mol Cancer Res, Mar 2015
Notably, the human CST complex (CTC1/STN1/TEN1), known to interact functionally with the polymerase complex (POLA/primase), was shown to be important for telomere processing.
The shelterin component TPP1 is a binding partner and substrate for the deubiquitinating enzyme USP7.
Lingner et al., Lausanne, Switzerland. In J Biol Chem, 2014
Ubiquitination of human TPP1 also had no detectable effects on known protein interactions of TPP1 with TIN2, POT1, the CTC1-STN1-TEN1 complex, and telomerase.
Role of STN1 and DNA polymerase α in telomere stability and genome-wide replication in Arabidopsis.
Riha et al., Vienna, Austria. In Plos Genet, 2014
The CST (Cdc13/CTC1-STN1-TEN1) complex was proposed to have evolved kingdom specific roles in telomere capping and replication.
POT1a and components of CST engage telomerase and regulate its activity in Arabidopsis.
Shippen et al., College Station, United States. In Plos Genet, 2014
Here we further dissect the function of POT1a and explore its interplay with the CST (CTC1/STN1/TEN1) telomere complex.
Extending the model of Arabidopsis telomere length and composition across Brassicaceae.
Beilstein et al., Tucson, United States. In Chromosome Res, 2014
In addition, we used a phylogenetic approach to infer the evolutionary history of putative telomere-binding proteins, CTC1, STN1, TEN1 (CST), telomere repeat-binding factor like (TRFL), and single Myb histone (SMH).
Human CST abundance determines recovery from diverse forms of DNA damage and replication stress.
Price et al., Cincinnati, United States. In Cell Cycle, 2013
Mammalian CST (CTC1-STN1-TEN1) is a telomere-associated complex that functions in telomere duplex replication and fill-in synthesis of the telomeric C-strand following telomerase action.
The CDC13-STN1-TEN1 complex stimulates Pol α activity by promoting RNA priming and primase-to-polymerase switch.
Hurwitz et al., New York City, United States. In Nat Commun, 2013
Emerging evidence suggests that Cdc13-Stn1-Ten1 (CST), an RPA-like ssDNA-binding complex, may regulate primase-Pol α (PP) activity at telomeres constitutively, and at other genomic locations under conditions of replication stress.
Human TEN1 maintains telomere integrity and functions in genome-wide replication restart.
Price et al., Cincinnati, United States. In J Biol Chem, 2013
TEN1 is a component of the mammalian CTC1-STN1-TEN1 complex.
Molecular basis of telomere syndrome caused by CTC1 mutations.
Lingner et al., Lausanne, Switzerland. In Genes Dev, 2013
CTC1 forms with STN1 and TEN1 a trimeric complex termed CST, which binds ssDNA, promotes telomere DNA synthesis, and inhibits telomerase-mediated telomere elongation.
Yeast telomere maintenance is globally controlled by programmed ribosomal frameshifting and the nonsense-mediated mRNA decay pathway.
Dinman et al., College Park, United States. In Translation (austin), 2013
Functional -1 PRF signals were identified in the mRNAs encoding two components of yeast telomerase, EST1 and EST2, and in mRNAs encoding proteins involved in recruiting telomerase to chromosome ends, STN1 and CDC13.
The human CST complex is a terminator of telomerase activity.
Impact
Lingner et al., Lausanne, Switzerland. In Nature, 2012
Here we show that the human CST (CTC1, STN1 and TEN1) complex, previously implicated in telomere protection and DNA metabolism, inhibits telomerase activity through primer sequestration and physical interaction with the protection of telomeres 1 (POT1)–TPP1 telomerase processivity factor.
Telomere capping proteins are structurally related to RPA with an additional telomere-specific domain.
GeneRIF
Wuttke et al., Boulder, United States. In Proc Natl Acad Sci U S A, 2009
the crystal structures of the C-terminal domain of the Saccharomyces cerevisiae Stn1 and the Schizosaccharomyces pombe Ten1 proteins are reported.
Yeast telomere capping protein Stn1 overrides DNA replication control through the S phase checkpoint.
GeneRIF
Nugent et al., Riverside, United States. In Proc Natl Acad Sci U S A, 2009
Stn1 overrides DNA replication control through the S phase checkpoint
Distinct roles for yeast Stn1 in telomere capping and telomerase inhibition.
GeneRIF
Shore et al., Genève, Switzerland. In Embo J, 2008
The N terminus of Stn1 interacts with Ten1 and carries out its essential capping function. The C terminus of Stn1 binds both Cdc13 and Pol12.
The role of Stn1p in Saccharomyces cerevisiae telomere capping can be separated from its interaction with Cdc13p.
GeneRIF
Nugent et al., Riverside, United States. In Genetics, 2007
identified distinct Stn1p domains that mediate interaction with either Ten1p or Cdc13p, allowing analysis of whether the interaction between Cdc13p and Stn1p is indeed essential for telomere capping or length regulation
RPA-like proteins mediate yeast telomere function.
GeneRIF
Lundblad et al., Los Angeles, United States. In Nat Struct Mol Biol, 2007
Stn1 and Ten1 are DNA-binding proteins with specificity for telomeric DNA substrates.
Chromosome end protection plasticity revealed by Stn1p and Ten1p bypass of Cdc13p.
Impact
Nugent et al., Riverside, United States. In Nat Cell Biol, 2006
Two Cdc13-interacting proteins, Stn1p and Ten1p, are also required for viability and telomere length regulation.
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