TTBK2: A Tau Protein Kinase beyond Tau Phosphorylation.
Tau tubulin kinase 2 (TTBK2) is a kinase known to phosphorylate tau and tubulin. It has recently drawn much attention due to its involvement in multiple important cellular processes. Here, we review the current understanding of TTBK2, including its sequence, structure, binding sites, phosphorylation...
| Publicado en: | BioMed Research International Vol. 2015; pp. 1 - 11 |
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| Autores principales: | , , , , |
| Formato: | pictorial review tables/charts Journal Article |
| Publicado: |
Wiley-Blackwell
4/9/2015
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=109273919&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 109273919 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 23146133 FT2T jtl: BioMed Research International issn: 23146133 maglogo: N pubinfo: dt: 4/9/2015 vid: 2015 pid: 480 pub: Wiley-Blackwell place: Malden, Massachusetts artinfo: ui: 109273919 109273919 109273919 10.1155/2015/575170 109273919 ppf: 1 ppct: 10 formats: fmt: @attributes: type: P tig: atl: TTBK2: A Tau Protein Kinase beyond Tau Phosphorylation. aug: au: Liao, Jung-Chi Yang, T. Tony Weng, Rueyhung Roc Kuo, Ching-Te Chang, Chih-Wei affil: Institute of Atomic and Molecular Sciences, Academia Sinica, No. 1, Roosevelt Road, Section 4, Taipei 10617, Taiwan sug: subj: Protein Kinases Metabolism Phosphorylation Mutation Cell Physiology Models, Biological Protein Kinases Physiology Spinocerebellar Ataxias Physiopathology Spinocerebellar Ataxias Familial and Genetic Intracellular Signaling Peptides and Proteins Metabolism Sequence Analysis ab: Tau tubulin kinase 2 (TTBK2) is a kinase known to phosphorylate tau and tubulin. It has recently drawn much attention due to its involvement in multiple important cellular processes. Here, we review the current understanding of TTBK2, including its sequence, structure, binding sites, phosphorylation substrates, and cellular processes involved. TTBK2 possesses a casein kinase 1 (CK1) kinase domain followed by a ~900 amino acid segment, potentially responsible for its localization and substrate recruitment. It is known to bind to CEP164, a centriolar protein, and EB1, a microtubule plus-end tracking protein. In addition to autophosphorylation, known phosphorylation substrates of TTBK2 include tau, tubulin, CEP164, CEP97, and TDP-43, a neurodegeneration-associated protein. Mutations of TTBK2 are associated with spinocerebellar ataxia type 11. In addition, TTBK2 is essential for regulating the growth of axonemal microtubules in ciliogenesis. It also plays roles in resistance of cancer target therapies and in regulating glucose and GABA transport. Reported sites of TTBK2 localization include the centriole/basal body, the midbody, and possibly the mitotic spindles. Together, TTBK2 is a multifunctional kinase involved in important cellular processes and demands augmented efforts in investigating its functions. pubtype: Academic Journal doctype: pictorial review tables/charts Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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