Polarity reveals intrinsic cell chirality.

Polarity reveals intrinsic cell chirality. Research Abstract Details 

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Polarity reveals intrinsic cell chirality. Abstract Text:

Jingsong Xu,Alexandra Van Keymeulen,Nicole M Wakida,Pete Carlton,Michael W Berns,Henry R Bourne,

Like blood neutrophils, dHL60 cells respond to a uniform concentration of attractant by polarizing in apparently random directions. How each cell chooses its own direction is unknown. We now find that an arrow drawn from the center of the nucleus of an unpolarized cell to its centrosome strongly predicts the subsequent direction of attractant-induced polarity: Of 60 cells that polarized in response to uniform f-Met-Leu-Phe (fMLP), 42 polarized to the left of this arrow, 6 polarized to the right, and 12 polarized directly toward or away from the centrosome. To investigate this directional bias we perturbed a regulatory pathway, downstream of Cdc42 and partitioning-defective 6 (Par6), which controls centrosome orientation relative to polarity of other cells. Dominant negative Par6 mutants block polarity altogether, as previously shown for disrupting Cdc42 activity. Cells remain able to polarize, but without directional bias, if their microtubules are disrupted with nocodazole, or they express mutant proteins that interfere with activities of PKCzeta or dynein. Expressing constitutively active glycogen synthase kinase 3beta (GSK3beta) causes cells to polarize preferentially to the right. Distributions of most of these polarity regulators localize to the centrosome but show no left-right asymmetry before polarization. Together, these findings suggest that an intrinsically chiral structure, perhaps the centrosome, serves as a template for directing polarity in the absence of spatial cues. Such a template could help to determine left-right asymmetry and planar polarity in development.

Polarity reveals intrinsic cell chirality. Publishing Authors By Initials

J Xu,A Van Keymeulen,NM Wakida,P Carlton,MW Berns,HR Bourne,

For similar enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: rho gtp-binding proteins: cdc42 gtp-binding protein research abstracts see: enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: rho gtp-binding proteins: cdc42 gtp-binding protein research

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Polarity reveals intrinsic cell chirality. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 104

Page Numbers: 9296-300

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 0027-8424

DAY: 17

MONTH: 05

YEAR: 2007

Polarity reveals intrinsic cell chirality. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7505876

Polarity reveals intrinsic cell chirality. Keywords Mesh Terms:

KEYWORDS: cdc42 GTP-Binding Protein

MESH TERMS: metabolism

Chemical & Substance for Abstract: Polarity reveals intrinsic cell chirality. Information

Substance Name: cdc42 GTP-Binding Protein

Registry Number: EC 3.6.5.2

Grant and Affiliation Information for Polarity reveals intrinsic cell chirality.

AFFILIATION: Departments of Cellular and Molecular Pharmacology, School of Medicine, University of California-San Francisco, CA 94158, USA. jingsong@uic.edu

Country: United States

AGENCY: United States NCRR

GRANT: R01 RR 14892

ACRONYM: RR

MEDLINETA: Proc Natl Acad Sci U S A

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