title: TIN2, a new regulator of telomere length in human cells.
abstract: Telomeres are DNA-protein structures that cap linear chromosomes and are essential for maintaining genomic stability and cell phenotype. We identified a novel human telomere-associated protein, TIN2, by interaction cloning using the telomeric DNA-binding-protein TRF1 as a bait. TIN2 interacted with TRF1 in vitro and in cells, and co-localized with TRF1 in nuclei and metaphase chromosomes. A mutant TIN2 that lacks amino-terminal sequences effects elongated human telomeres in a telomerase-dependent manner. Our findings suggest that TRF1 is insufficient for control of telomere length in human cells, and that TIN2 is an essential mediator of TRF1 function.
authors.affiliation: Department of Cell and Molecular Biology, Lawrence Berkeley National Laboratory, Berkeley, California, USA.
authors.forename: S H
authors.initials: SH
authors.lastname: Kim
authors.forename: P
authors.initials: P
authors.lastname: Kaminker
authors.forename: J
authors.initials: J
authors.lastname: Campisi
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D015870:Gene Expression; D006801:Humans; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion; D016615:Telomere / Q000235:genetics* / Q000378:metabolism*; D034501:Telomere-Binding Proteins; D035321:Telomeric Repeat Binding Protein 1; D014018:Tissue Distribution
chemical_list: D018076:DNA, Complementary; D004268:DNA-Binding Proteins; D012333:RNA, Messenger; D011994:Recombinant Proteins; C440868:TINF2 protein, human; D034501:Telomere-Binding Proteins; D035321:Telomeric Repeat Binding Protein 1