A functional cooperativity between Aurora A kinase and LIM kinase1 Implication in the mitotic process

    Authors

    L. Ritchey; R. Ottman; M. Roumanos;R. Chakrabarti

    Comments

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    Abbreviated Journal Title

    Cell Cycle

    Keywords

    LIMK1; Aurora A; mitotic spindle; phosphorylation; PROSTATE EPITHELIAL-CELLS; ADVANCED SOLID TUMORS; A KINASE; COFILIN; PHOSPHORYLATION; PROTEIN-KINASE; SELECTIVE INHIBITOR; SPINDLE FORMATION; ACTIN DYNAMICS; GAMMA-TUBULIN; ACTIVATION; Cell Biology

    Abstract

    Aurora kinase A (Aur-A), a mitotic kinase, regulates initiation of mitosis through centrosome separation and proper assembly of bipolar spindles. LIM kinase 1 (LIMK1), a modulator of actin and microtubule dynamics, is involved in the mitotic process through inactivating phosphorylation of cofilin. Phosphorylated LIMK1 is recruited to the centrosomes during early prophase, where it colocalizes with gamma-tubulin. Here, we report a novel functional cooperativity between Aur-A and LIMK1 through mutual phosphorylation. LIMK1 is recruited to the centrosomes during early prophase and then to the spindle poles, where it colocalizes with Aur-A. Aur-A physically associates with LIMK1 and activates it through phosphorylation, which is important for its centrosomal and spindle pole localization. Aur-A also acts as a substrate of LIMK1, and the function of LIMK1 is important for its specific localization and regulation of spindle morphology. Taken together, the novel molecular interaction between these two kinases and their regulatory roles on one other's function may provide new insight on the role of Aur-A in manipulation of actin and microtubular structures during spindle formation.

    Journal Title

    Cell Cycle

    Volume

    11

    Issue/Number

    2

    Publication Date

    1-1-2012

    Document Type

    Article

    Language

    English

    First Page

    296

    Last Page

    309

    WOS Identifier

    WOS:000299164200021

    ISSN

    1538-4101

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