FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2079016687> ?p ?o ?g. }

• W2079016687 endingPage "24187" @default.
• W2079016687 startingPage "24180" @default.
• W2079016687 abstract "The single-stranded DNA binding proteins in mouse shelterin, POT1a and POT1b, accumulate at telomeres as heterodimers with TPP1, which binds TIN2 and thus links the TPP1/POT1 dimers with TRF1 and TRF2/Rap1. When TPP1 is tethered to TIN2/TRF1/TRF2, POT1a is thought to block replication protein A binding to the single-stranded telomeric DNA and prevent ataxia telangiectasia and Rad3-related kinase activation. Similarly, TPP1/POT1b tethered to TIN2 can control the formation of the correct single-stranded telomeric overhang. Consistent with this view, the telomeric phenotypes following deletion of POT1a,b or TPP1 are phenocopied in TIN2-deficient cells. However, the loading of TRF1 and TRF2/Rap1 is additionally compromised in TIN2 KO cells, leading to added phenotypes. Therefore, it could not be excluded that, in addition to TIN2, other components of shelterin contribute to the recruitment of TPP1/POT1a,b as suggested by previous reports. To test whether TIN2 is the sole link between TPP1/POT1a,b and telomeres, we defined the TPP1 interaction domain of TIN2 and generated a TIN2 allele that was unable to interact with TPP1 but retained its interaction with TRF1 and TRF2. We demonstrated that cells expressing TIN2ΔTPP1 instead of wild-type TIN2 phenocopy the POT1a,b knockout setting without showing additional phenotypes. Therefore, these results are consistent with TIN2 being the only mechanism by which TPP1/POT1 heterodimers bind to shelterin and function in telomere protection. The single-stranded DNA binding proteins in mouse shelterin, POT1a and POT1b, accumulate at telomeres as heterodimers with TPP1, which binds TIN2 and thus links the TPP1/POT1 dimers with TRF1 and TRF2/Rap1. When TPP1 is tethered to TIN2/TRF1/TRF2, POT1a is thought to block replication protein A binding to the single-stranded telomeric DNA and prevent ataxia telangiectasia and Rad3-related kinase activation. Similarly, TPP1/POT1b tethered to TIN2 can control the formation of the correct single-stranded telomeric overhang. Consistent with this view, the telomeric phenotypes following deletion of POT1a,b or TPP1 are phenocopied in TIN2-deficient cells. However, the loading of TRF1 and TRF2/Rap1 is additionally compromised in TIN2 KO cells, leading to added phenotypes. Therefore, it could not be excluded that, in addition to TIN2, other components of shelterin contribute to the recruitment of TPP1/POT1a,b as suggested by previous reports. To test whether TIN2 is the sole link between TPP1/POT1a,b and telomeres, we defined the TPP1 interaction domain of TIN2 and generated a TIN2 allele that was unable to interact with TPP1 but retained its interaction with TRF1 and TRF2. We demonstrated that cells expressing TIN2ΔTPP1 instead of wild-type TIN2 phenocopy the POT1a,b knockout setting without showing additional phenotypes. Therefore, these results are consistent with TIN2 being the only mechanism by which TPP1/POT1 heterodimers bind to shelterin and function in telomere protection." @default.
• W2079016687 created "2016-06-24" @default.
• W2079016687 creator A5040802717 @default.
• W2079016687 creator A5065113600 @default.
• W2079016687 date "2014-08-01" @default.
• W2079016687 modified "2023-10-18" @default.
• W2079016687 title "Binding of TPP1 Protein to TIN2 Protein Is Required for POT1a,b Protein-mediated Telomere Protection" @default.
• W2079016687 cites W1972655555 @default.
• W2079016687 cites W1982199027 @default.
• W2079016687 cites W1996946708 @default.
• W2079016687 cites W1999334180 @default.
• W2079016687 cites W2003446723 @default.
• W2079016687 cites W2003718497 @default.
• W2079016687 cites W2023875413 @default.
• W2079016687 cites W2027931017 @default.
• W2079016687 cites W2028320710 @default.
• W2079016687 cites W2029860584 @default.
• W2079016687 cites W2035389897 @default.
• W2079016687 cites W2056891782 @default.
• W2079016687 cites W2058375396 @default.
• W2079016687 cites W2065434335 @default.
• W2079016687 cites W2072744580 @default.
• W2079016687 cites W2082435463 @default.
• W2079016687 cites W2084960769 @default.
• W2079016687 cites W2090517238 @default.
• W2079016687 cites W2100756422 @default.
• W2079016687 cites W2107010359 @default.
• W2079016687 cites W2110565388 @default.
• W2079016687 cites W2124139300 @default.
• W2079016687 cites W2127539269 @default.
• W2079016687 cites W2145952889 @default.
• W2079016687 cites W2148949291 @default.
• W2079016687 cites W2149058300 @default.
• W2079016687 cites W2150490516 @default.
• W2079016687 cites W2153633026 @default.
• W2079016687 cites W2170632126 @default.
• W2079016687 doi "https://doi.org/10.1074/jbc.m114.592592" @default.
• W2079016687 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4148849" @default.
• W2079016687 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25056954" @default.
• W2079016687 hasPublicationYear "2014" @default.
• W2079016687 type Work @default.
• W2079016687 sameAs 2079016687 @default.
• W2079016687 citedByCount "42" @default.
• W2079016687 countsByYear W20790166872014 @default.
• W2079016687 countsByYear W20790166872015 @default.
• W2079016687 countsByYear W20790166872016 @default.
• W2079016687 countsByYear W20790166872017 @default.
• W2079016687 countsByYear W20790166872018 @default.
• W2079016687 countsByYear W20790166872019 @default.
• W2079016687 countsByYear W20790166872020 @default.
• W2079016687 countsByYear W20790166872021 @default.
• W2079016687 countsByYear W20790166872022 @default.
• W2079016687 countsByYear W20790166872023 @default.
• W2079016687 crossrefType "journal-article" @default.
• W2079016687 hasAuthorship W2079016687A5040802717 @default.
• W2079016687 hasAuthorship W2079016687A5065113600 @default.
• W2079016687 hasBestOaLocation W20790166871 @default.
• W2079016687 hasConcept C104317684 @default.
• W2079016687 hasConcept C127716648 @default.
• W2079016687 hasConcept C143425029 @default.
• W2079016687 hasConcept C153911025 @default.
• W2079016687 hasConcept C177336024 @default.
• W2079016687 hasConcept C202265312 @default.
• W2079016687 hasConcept C2776179587 @default.
• W2079016687 hasConcept C2776879488 @default.
• W2079016687 hasConcept C54355233 @default.
• W2079016687 hasConcept C552990157 @default.
• W2079016687 hasConcept C62478195 @default.
• W2079016687 hasConcept C86339819 @default.
• W2079016687 hasConcept C86803240 @default.
• W2079016687 hasConcept C94966510 @default.
• W2079016687 hasConcept C95444343 @default.
• W2079016687 hasConceptScore W2079016687C104317684 @default.
• W2079016687 hasConceptScore W2079016687C127716648 @default.
• W2079016687 hasConceptScore W2079016687C143425029 @default.
• W2079016687 hasConceptScore W2079016687C153911025 @default.
• W2079016687 hasConceptScore W2079016687C177336024 @default.
• W2079016687 hasConceptScore W2079016687C202265312 @default.
• W2079016687 hasConceptScore W2079016687C2776179587 @default.
• W2079016687 hasConceptScore W2079016687C2776879488 @default.
• W2079016687 hasConceptScore W2079016687C54355233 @default.
• W2079016687 hasConceptScore W2079016687C552990157 @default.
• W2079016687 hasConceptScore W2079016687C62478195 @default.
• W2079016687 hasConceptScore W2079016687C86339819 @default.
• W2079016687 hasConceptScore W2079016687C86803240 @default.
• W2079016687 hasConceptScore W2079016687C94966510 @default.
• W2079016687 hasConceptScore W2079016687C95444343 @default.
• W2079016687 hasFunder F4320332161 @default.
• W2079016687 hasIssue "35" @default.
• W2079016687 hasLocation W20790166871 @default.
• W2079016687 hasLocation W20790166872 @default.
• W2079016687 hasLocation W20790166873 @default.
• W2079016687 hasLocation W20790166874 @default.
• W2079016687 hasOpenAccess W2079016687 @default.
• W2079016687 hasPrimaryLocation W20790166871 @default.
• W2079016687 hasRelatedWork W1985964699 @default.
• W2079016687 hasRelatedWork W1996800742 @default.
• W2079016687 hasRelatedWork W2003718497 @default.

• next