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          Institute: MPI für biophysikalische Chemie     Collection: Biochemie und Zellbiologie (Prof. Klaus Weber)     Display Documents



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ID: 16704.0, MPI für biophysikalische Chemie / Biochemie und Zellbiologie (Prof. Klaus Weber)
The mitotic-spindle-associated protein astrin is essential for progression through mitosis
Authors:Gruber, J.; Harborth, J.; Schnabel, J.; Weber, K.; Hatzfeld, M.
Language:English
Date of Publication (YYYY-MM-DD):2002-11-01
Title of Journal:Journal of Cell Science
Volume:115
Issue / Number:21
Start Page:4053
End Page:4059
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Astrin is a mitotic-spindle-associated protein expressed in most human cell lines and tissues. However, its functions in spindle organization and mitosis have not yet been determined. Sequence analysis revealed that astrin has an N-terminal globular domain and an extended coiled-coil domain. Recombinant astrin was purified and characterized by CD spectroscopy and electron microscopy. Astrin showed parallel dimers with head- stalk structures reminiscent of motor proteins, although no sequence similarities to known motor proteins were found. In physiological buffers, astrin dimers oligomerized via their globular head domains and formed aster-like structures. Silencing of astrin in HeLa cells by RNA interference resulted in growth arrest, with formation of multipolar and highly disordered spindles. Chromosomes did not congress to the spindle equator and remained dispersed. Cells depleted of astrin were normal during interphase but were unable to progress through mitosis and finally ended in apoptotic cell death. Possible functions of astrin in mitotic spindle organization are discussed.
Free Keywords:astrin; coiled coil; microtubules; mitotic spindle; RNA; interference
Comment of the Author/Creator:Date: 2002, NOV 1
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Klaus Weber / 090
External Affiliations:Univ Halle Wittenberg, Fac Med, Dept Biochem & Pathobiochem, D-; 06097 Halle Saale, Germany; Univ Halle Wittenberg, Fac Med, Dept Biochem & Pathobiochem, D-06097 Halle Saale, Germany
Identifiers:URL:http://jcs.biologists.org/cgi/reprint/115/21/4053
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