The dynamic protein Knl1 - a kinetochore rendezvous

被引:34
作者
Ghongane, Priyanka [1 ]
Kapanidou, Maria [1 ]
Asghar, Adeel [2 ]
Elowe, Sabine [2 ]
Bolanos-Garcia, Victor M. [1 ]
机构
[1] Oxford Brookes Univ, Fac Hlth & Life Sci, Dept Biol & Med Sci, Oxford OX3 0BP, England
[2] CHUQ, Ctr Rech, Quebec City, PQ G1V 4G2, Canada
关键词
BubR1; Knl1; MELT motif; Kinetochore; Mitosis; Mitotic checkpoint; SPINDLE ASSEMBLY CHECKPOINT; INTRINSICALLY DISORDERED PROTEINS; AURORA B KINASE; MITOTIC CHECKPOINT; OUTER KINETOCHORE; CHROMOSOME SEGREGATION; MICROTUBULE-BINDING; SKA COMPLEX; B56-PP2A PHOSPHATASE; STRUCTURAL-ANALYSIS;
D O I
10.1242/jcs.149922
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Knl1 (also known as CASC5, UniProt Q8NG31) is an evolutionarily conserved scaffolding protein that is required for proper kinetochore assembly, spindle assembly checkpoint (SAC) function and chromosome congression. A number of recent reports have confirmed the prominence of Knl1 in these processes and provided molecular details and structural features that dictate Knl1 functions in higher organisms. Knl1 recruits SAC components to the kinetochore and is the substrate of certain protein kinases and phosphatases, the interplay of which ensures the exquisite regulation of the aforementioned processes. In this Commentary, we discuss the overall domain organization of Knl1 and the roles of this protein as a versatile docking platform. We present emerging roles of the protein interaction motifs present in Knl1, including the RVSF, SILK, MELT and KI motifs, and their role in the recruitment and regulation of the SAC proteins Bub1, BubR1, Bub3 and Aurora B. Finally, we explore how the regions of low structural complexity that characterize Knl1 are implicated in the cooperative interactions that mediate binding partner recognition and scaffolding activity by Knl1.
引用
收藏
页码:3415 / 3423
页数:9
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