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Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization. / Fielding, Andrew B.; Dobreva, Iveta; McDonald, Paul C et al.
In: Journal of Cell Biology, Vol. 180, No. 4, 25.02.2008, p. 681-9.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Fielding, AB, Dobreva, I, McDonald, PC, Foster, LJ & Dedhar, S 2008, 'Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization', Journal of Cell Biology, vol. 180, no. 4, pp. 681-9. https://doi.org/10.1083/jcb.200710074

APA

Fielding, A. B., Dobreva, I., McDonald, P. C., Foster, L. J., & Dedhar, S. (2008). Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization. Journal of Cell Biology, 180(4), 681-9. https://doi.org/10.1083/jcb.200710074

Vancouver

Fielding AB, Dobreva I, McDonald PC, Foster LJ, Dedhar S. Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization. Journal of Cell Biology. 2008 Feb 25;180(4):681-9. doi: 10.1083/jcb.200710074

Author

Fielding, Andrew B. ; Dobreva, Iveta ; McDonald, Paul C et al. / Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization. In: Journal of Cell Biology. 2008 ; Vol. 180, No. 4. pp. 681-9.

Bibtex

@article{22414281f9ed4c4f8eed914d85ddc8d0,
title = "Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization",
abstract = "Integrin-linked kinase (ILK) is a serine-threonine kinase and scaffold protein with well defined roles in focal adhesions in integrin-mediated cell adhesion, spreading, migration, and signaling. Using mass spectrometry-based proteomic approaches, we identify centrosomal and mitotic spindle proteins as interactors of ILK. alpha- and beta-tubulin, ch-TOG (XMAP215), and RUVBL1 associate with ILK and colocalize with it to mitotic centrosomes. Inhibition of ILK activity or expression induces profound apoptosis-independent defects in the organization of the mitotic spindle and DNA segregation. ILK fails to localize to the centrosomes of abnormal spindles in RUVBL1-depleted cells. Additionally, depletion of ILK expression or inhibition of its activity inhibits Aurora A-TACC3/ch-TOG interactions, which are essential for spindle pole organization and mitosis. These data demonstrate a critical and unexpected function for ILK in the organization of centrosomal protein complexes during mitotic spindle assembly and DNA segregation.",
keywords = "ATPases Associated with Diverse Cellular Activities, Aurora Kinases, Carrier Proteins, Centrosome, Chromosome Segregation, DNA Helicases, Down-Regulation, HeLa Cells, Humans, Mass Spectrometry, Microtubule-Associated Proteins, Mitosis, Nuclear Proteins, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Spindle Apparatus, Tubulin, Journal Article, Research Support, Non-U.S. Gov't",
author = "Fielding, {Andrew B.} and Iveta Dobreva and McDonald, {Paul C} and Foster, {Leonard J} and Shoukat Dedhar",
year = "2008",
month = feb,
day = "25",
doi = "10.1083/jcb.200710074",
language = "English",
volume = "180",
pages = "681--9",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "4",

}

RIS

TY - JOUR

T1 - Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization

AU - Fielding, Andrew B.

AU - Dobreva, Iveta

AU - McDonald, Paul C

AU - Foster, Leonard J

AU - Dedhar, Shoukat

PY - 2008/2/25

Y1 - 2008/2/25

N2 - Integrin-linked kinase (ILK) is a serine-threonine kinase and scaffold protein with well defined roles in focal adhesions in integrin-mediated cell adhesion, spreading, migration, and signaling. Using mass spectrometry-based proteomic approaches, we identify centrosomal and mitotic spindle proteins as interactors of ILK. alpha- and beta-tubulin, ch-TOG (XMAP215), and RUVBL1 associate with ILK and colocalize with it to mitotic centrosomes. Inhibition of ILK activity or expression induces profound apoptosis-independent defects in the organization of the mitotic spindle and DNA segregation. ILK fails to localize to the centrosomes of abnormal spindles in RUVBL1-depleted cells. Additionally, depletion of ILK expression or inhibition of its activity inhibits Aurora A-TACC3/ch-TOG interactions, which are essential for spindle pole organization and mitosis. These data demonstrate a critical and unexpected function for ILK in the organization of centrosomal protein complexes during mitotic spindle assembly and DNA segregation.

AB - Integrin-linked kinase (ILK) is a serine-threonine kinase and scaffold protein with well defined roles in focal adhesions in integrin-mediated cell adhesion, spreading, migration, and signaling. Using mass spectrometry-based proteomic approaches, we identify centrosomal and mitotic spindle proteins as interactors of ILK. alpha- and beta-tubulin, ch-TOG (XMAP215), and RUVBL1 associate with ILK and colocalize with it to mitotic centrosomes. Inhibition of ILK activity or expression induces profound apoptosis-independent defects in the organization of the mitotic spindle and DNA segregation. ILK fails to localize to the centrosomes of abnormal spindles in RUVBL1-depleted cells. Additionally, depletion of ILK expression or inhibition of its activity inhibits Aurora A-TACC3/ch-TOG interactions, which are essential for spindle pole organization and mitosis. These data demonstrate a critical and unexpected function for ILK in the organization of centrosomal protein complexes during mitotic spindle assembly and DNA segregation.

KW - ATPases Associated with Diverse Cellular Activities

KW - Aurora Kinases

KW - Carrier Proteins

KW - Centrosome

KW - Chromosome Segregation

KW - DNA Helicases

KW - Down-Regulation

KW - HeLa Cells

KW - Humans

KW - Mass Spectrometry

KW - Microtubule-Associated Proteins

KW - Mitosis

KW - Nuclear Proteins

KW - Protein Structure, Tertiary

KW - Protein-Serine-Threonine Kinases

KW - Spindle Apparatus

KW - Tubulin

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1083/jcb.200710074

DO - 10.1083/jcb.200710074

M3 - Journal article

C2 - 18283114

VL - 180

SP - 681

EP - 689

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 4

ER -