The 68-kDa Telomeric Repeat Binding Factor 1 (TRF1)-associated Protein (TAP68) Interacts with and Recruits TRF1 to the Spindle Pole during Mitosis

Lan, Jianping; Zhu, Yuanyuan; Xu, Leilei; Yu, Huijuan; Yu, Jian; Liu, Xing; Fu, Chuanhai; Wang, Xiaogang; Ke, Youqi; Huang, He; Dou, Zhen

doi:10.1074/jbc.m113.526244

Cited by 9 publications

(17 citation statements)

References 54 publications

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“…This results from the existence of two different potential start codons, 59 amino acids apart from each other, and means that full length TRIOBP-1 can be either 593 or 652 amino acids in length [12]. The 593 amino acid long version of TRIOBP-1 was the first TRIOBP protein to be described, under the name TARA, for TRIO Associated Repeat on Actin [3] (also referred to as TAP68 [14]). This appears to be the more abundant species in many cell culture systems.…”

Section: The Structure Of Triobp-1mentioning

confidence: 99%

The TRIOBP Isoforms and Their Distinct Roles in Actin Stabilization, Deafness, Mental Illness, and Cancer

2020

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The TRIOBP (TRIO and F-actin Binding Protein) gene encodes multiple proteins, which together play crucial roles in modulating the assembly of the actin cytoskeleton. Splicing of the TRIOBP gene is complex, with the two most studied TRIOBP protein isoforms sharing no overlapping amino acid sequence with each other. TRIOBP-1 (also known as TARA or TAP68) is a mainly structured protein that is ubiquitously expressed and binds to F-actin, preventing its depolymerization. It has been shown to be important for many processes including in the cell cycle, adhesion junctions, and neuronal differentiation. TRIOBP-1 has been implicated in schizophrenia through the formation of protein aggregates in the brain. In contrast, TRIOBP-4 is an entirely disordered protein with a highly specialized expression pattern. It is known to be crucial for the bundling of actin in the stereocilia of the inner ear, with mutations in it causing severe or profound hearing loss. Both of these isoforms are implicated in cancer. Additional longer isoforms of TRIOBP exist, which overlap with both TRIOBP-1 and 4. These appear to participate in the functions of both shorter isoforms, while also possessing unique functions in the inner ear. In this review, the structures and functions of all of these isoforms are discussed, with a view to understanding how they operate, both alone and in combination, to modulate actin and their consequences for human illness.

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Section: The Structure Of Triobp-1mentioning

confidence: 99%

The TRIOBP Isoforms and Their Distinct Roles in Actin Stabilization, Deafness, Mental Illness, and Cancer

2020

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“…Tankyrases are segregated to multiple cellular locations. In human cells, TNKS has been found at telomeres [ 9 , 11 ], at nuclear pores [ 102 ], at the Golgi complex [ 59 , 82 , 103 ], in the cytoplasm [ 18 ], at the cell membrane [ 104 ] and at the spindle poles [ 97 , 103 , 105 - 108 ]. The dynamic sub-cellular localizations of Tankyrases as well as their posttranslational protein modifications will influence protein/protein interactions.…”

Section: Cellular Roles Of Tankyrasesmentioning

confidence: 99%

Tankyrases: Structure, Function and Therapeutic Implications in Cancer

Haikarainen¹,

Krauß²,

Lehtiö³

2014

CPD

163

195

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Several cellular signaling pathways are regulated by ADP-ribosylation, a posttranslational modification catalyzed by members of the ARTD superfamily. Tankyrases are distinguishable from the rest of this family by their unique domain organization, notably the sterile alpha motif responsible for oligomerization and ankyrin repeats mediating protein-protein interactions. Tankyrases are involved in various cellular functions, such as telomere homeostasis, Wnt/β-catenin signaling, glucose metabolism, and cell cycle progression. In these processes, Tankyrases regulate the interactions and stability of target proteins by poly (ADP-ribosyl)ation. Modified proteins are subsequently recognized by the E3 ubiquitin ligase RNF146, poly-ubiquitinated and predominantly guided to 26S proteasomal degradation. Several small molecule inhibitors have been described for Tankyrases; they compete with the co-substrate NAD+ for binding to the ARTD catalytic domain. The recent, highly potent and selective inhibitors possess several properties of lead compounds and can be used for proof-of-concept studies in cancer and other Tankyrase linked diseases.

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“…TERRA has been found mainly in the nucleus, although cytoplasmic localization of shelterin proteins has been reported [20][21][22]. Interestingly, extranuclear TERRA foci have been detected in human cancer cell line after knockdown of retrotransposon Long Interspersed Nuclear Element 1 (LINE1) [23].…”

Section: Introductionmentioning

confidence: 99%

Loss of telomere silencing is accompanied by dysfunction of Polo kinase and centrosomes during Drosophila oogenesis and early development

et al. 2021

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Telomeres are nucleoprotein complexes that protect the ends of eukaryotic linear chromosomes from degradation and fusions. Telomere dysfunction leads to cell growth arrest, oncogenesis, and premature aging. Telomeric RNAs have been found in all studied species; however, their functions and biogenesis are not clearly understood. We studied the mechanisms of development disorders observed upon overexpression of telomeric repeats in Drosophila. In somatic cells, overexpression of telomeric retrotransposon HeT-A is cytotoxic and leads to the accumulation of HeT-A Gag near centrosomes. We found that RNA and RNA-binding protein Gag encoded by the telomeric retrotransposon HeT-A interact with Polo and Cdk1 mitotic kinases, which are conserved regulators of centrosome biogenesis and cell cycle. The depletion of proteins Spindle E, Ccr4 or Ars2 resulting in HeT-A overexpression in the germline was accompanied by mislocalization of Polo as well as its abnormal stabilization during oogenesis and severe deregulation of centrosome biogenesis leading to maternal-effect embryonic lethality. These data suggest a mechanistic link between telomeric HeT-A ribonucleoproteins and cell cycle regulators that ensures the cell response to telomere dysfunction.

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The 68-kDa Telomeric Repeat Binding Factor 1 (TRF1)-associated Protein (TAP68) Interacts with and Recruits TRF1 to the Spindle Pole during Mitosis

Cited by 9 publications

References 54 publications

The TRIOBP Isoforms and Their Distinct Roles in Actin Stabilization, Deafness, Mental Illness, and Cancer

The TRIOBP Isoforms and Their Distinct Roles in Actin Stabilization, Deafness, Mental Illness, and Cancer

Tankyrases: Structure, Function and Therapeutic Implications in Cancer

Loss of telomere silencing is accompanied by dysfunction of Polo kinase and centrosomes during Drosophila oogenesis and early development

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