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Details on Person Studies in yeast and human cells indicate that recruitment o...
| Class:Id | Summation:174908 |
|---|---|
| _displayName | Studies in yeast and human cells indicate that recruitment o... |
| _timestamp | 2020-05-04 16:28:18 |
| created | [InstanceEdit:174905] Gillespie, ME, 2006-02-22 18:57:46 |
| literatureReference | [LiteratureReference:177185] Cell cycle-regulated trafficking of human telomerase to telomeres [LiteratureReference:184155] Cdc13 delivers separate complexes to the telomere for end protection and replication [LiteratureReference:184157] Delivery of yeast telomerase to a DNA break depends on the recruitment functions of Cdc13 and Est1 [LiteratureReference:184122] Sequence-specific DNA primer effects on telomerase polymerization activity [LiteratureReference:184127] Oxcarbazepine does not interact with cimetidine in healthy volunteers [LiteratureReference:184125] Regulation of 5' template usage and incorporation of noncognate nucleotides by human telomerase [LiteratureReference:184123] The end of the (DNA) line [LiteratureReference:184147] Switching and signaling at the telomere [LiteratureReference:163093] Regulation of telomerase by telomeric proteins [LiteratureReference:182735] Est1p as a cell cycle-regulated activator of telomere-bound telomerase [LiteratureReference:184158] Telomeric protein distributions and remodeling through the cell cycle in Saccharomyces cerevisiae [LiteratureReference:177177] Cell cycle-dependent recruitment of telomerase RNA and Cajal bodies to human telomeres [LiteratureReference:9671168] A recessive founder mutation in regulator of telomere elongation helicase 1, RTEL1, underlies severe immunodeficiency and features of Hoyeraal Hreidarsson syndrome [LiteratureReference:9671174] Germline mutations of regulator of telomere elongation helicase 1, RTEL1, in Dyskeratosis congenita [LiteratureReference:9671180] Constitutional mutations in RTEL1 cause severe dyskeratosis congenita [LiteratureReference:9686596] Human RTEL1 deficiency causes Hoyeraal-Hreidarsson syndrome with short telomeres and genome instability [LiteratureReference:9686599] Inherited mutations in the helicase RTEL1 cause telomere dysfunction and Hoyeraal-Hreidarsson syndrome |
| modified | [InstanceEdit:177218] Gillespie, ME, 2006-03-24 04:31:14 [InstanceEdit:180778] Gillespie, ME, 2006-06-05 03:42:53 [InstanceEdit:183139] Gillespie, ME, 2006-07-21 18:01:36 [InstanceEdit:184154] Gopinathrao, G, 2006-07-24 19:18:08 [InstanceEdit:8940159] D'Eustachio, Peter, 2016-09-23 [InstanceEdit:9668590] Orlic-Milacic, Marija, 2019-11-28 [InstanceEdit:9670636] Orlic-Milacic, Marija, 2019-12-11 [InstanceEdit:9671096] Orlic-Milacic, Marija, 2019-12-18 [InstanceEdit:9671187] Orlic-Milacic, Marija, 2019-12-18 [InstanceEdit:9671188] Orlic-Milacic, Marija, 2019-12-18 [InstanceEdit:9686586] Orlic-Milacic, Marija, 2020-05-04 [InstanceEdit:9686607] Orlic-Milacic, Marija, 2020-05-04 |
| text | Studies in yeast and human cells indicate that recruitment of telomerase to a telomere may be influenced by multiple variables, including regulatory protein factors, hTERT domains, telomere length, and the cell cycle stage. First, in yeast, the telomerase associated factor Est1 and the single-strand DNA binding protein Cdc13 play roles in telomerase recruitment (Pennock et al. 2001; Bianchi et al. 2004). Analogous proteins exist in human cells (Est1A, Est1B, Est1C, and POT1, respectively); however, how or whether these proteins are directly involved in telomerase recruitment remains to be elucidated. Second, N-terminal residues of hTERT within the DAT (dissociate the activities of telomerase) domain may have a role in binding single stranded telomeric DNA as the "anchor site" (Lee et al. 1993; Moriarty et al. 2005). Third, a cis-acting mechanism in yeast and humans that regulates telomere length maintenance may modulate telomerase access to the telomere (reviewed in Blackburn 2001; Smogorzewska and de Lange, 2004). Long telomeres, which have more associated protein factors, are in a state that is acted on by telomerase less frequently than that of short telomeres, which have fewer associated factors. Whether short telomeres actively recruit telomerase remains to be determined. Last, the recruitment of telomerase to telomeres shows cell-cycle regulation (Taggart et al. 2002; Smith et al. 2003; Fisher et al. 2004; Jady et al. 2006; Tomlinson et al. 2006). Presence of the telomeric protection complex shelterin at telomeres is necessary for the recruitment of telomerase. ACD (TPP1), the subunit of the shelterin complex, directly interacts, through its TEL patch region, with telomerase and is required for telomerase function in vivo (Abreu et al. 2010, Nandakumar et al. 2012, Sexton et al. 2014). The interaction involves the TEN domain of TERT (Schmidt et al. 2014). The helicase RTEL1 is recruited to telomeres in S phase via direct interaction with the shelterin complex subunit TREF2. RTEL1 is needed for T-loop unwinding and resolution of telomeric G-quadruplex (G4) DNA structures, necessary steps for efficient telomere replication (Vannier et al. 2012, Sarek et al. 2015). Germline mutations in RTEL1 cause a severe form of dyskeratosis congenita, a telomere disorder syndrome, called Hoyeraal Hreidarsson syndrome (Ballew, Yeager et al. 2013; Walne et al. 2013; Ballew, Joseph et al. 2013, Le Guen et al. 2013, Deng et al. 2013). Loading of RTEL1 to telomere ends is negatively regulated outside of S phase by CDK2:CCNA-mediated phosphorylation of the shelterin complex subunit TERF2 at serine residue S365. At the S phase entry, TERF2 is dephosphorylated by the PP6 phosphatase, thus allowing timely RTEL1 loading (Sarek et al. 2019). |
| (summation) | [Reaction:163096] Recruitment of Telomerase RNP to the Telomeric Chromosome End [Homo sapiens] |
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