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Structural Plasticity in Actin and Tubulin Polymer Dynamics

This article provides information on recent findings on polymerization and depolymerization of actin filaments and microtubules. Actin filaments and microtubules polymerize and depolymerize by adding and removing subunits at polymer ends, and these dynamics drive cytoplasmic organization, cell division, and cell motility. Since Wegner proposed the treadmilling theory for actin in 1976, it has largely been assumed that the chemical state of the bound nucleotide determines the rates of subunit addition and removal. This chemical kinetics view is difficult to reconcile with observations revealing multiple structural states of the polymer that influence polymerization dynamics but that are not strictly coupled to the bound nucleotide state. We refer to these phenomena as ‚Äústructural plasticity‚ÄĚ and discuss emerging evidence that they play a central role in polymer dynamics and function.

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Classifications


Resource Type: Journal article/Issue, Illustration, Review
Audience Level: Undergraduate lower division 13-14, Undergraduate upper division 15-16, Graduate, Professional (degree program), Continuing education

Author and Copyright


Authors and Editors: Hao Yuan Kueh of Department of Systems Biology, Harvard Medical School, Timothy Mitchison of Graduate Program in Biophysics, Harvard University
Publisher: SCIENCE
Format: text/html
Copyright and other restrictions: Yes
Cost: No

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American Association for the Advancement of Science


     
   

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