Regulation of Nek6 Functions by Its SUMOylation on the K∨252 Residue

Nek6 belongs to NIMA1 (never in mitosis, gene A) related kinase, which was originally identified in Aspergillus nidulans as a serine/threonine kinase critical for cell cycle progression. We noticed that the putative SUMOylation site is localized on the K∨252 residue in ∨251FKsD∨254 of Nek6, based on...

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Veröffentlicht in:Integrative biosciences 2007-12, Vol.11 (2), p.205-213
Hauptverfasser: Lee, E.J. (Chungbuk National University, Cheongju, Republic of Korea), Hyun, S.H. (Eulji University School of Medicine, Daejeon, Republic of Korea), Chun, J.S. (Korea National University of Education, Cheongwon, Republic of Korea), Shin, S.H. (Chungbuk National University, Cheongju, Republic of Korea), Lee, K.E. (Chungbuk National University, Cheongju, Republic of Korea), Park, I.S. (Chungbuk National University, Cheongju, Republic of Korea), Kang, S.S. (Chungbuk National University, Cheongju, Republic of Korea), E-mail: jin95324@cbu.ac.kr
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Sprache:eng
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Zusammenfassung:Nek6 belongs to NIMA1 (never in mitosis, gene A) related kinase, which was originally identified in Aspergillus nidulans as a serine/threonine kinase critical for cell cycle progression. We noticed that the putative SUMOylation site is localized on the K∨252 residue in ∨251FKsD∨254 of Nek6, based on the consensus sequence ΦKxE; where Φ represents L, I, V or F and x is any amino acid. We observed that the Nek6 SUMO mutant (K252R) has decreased protein kinase activity, nuclear speckle localization and protein stability, compared with that of the Nek6 wild type.
ISSN:1738-6357
DOI:10.1080/17386357.2007.9647337