CLASP promotes microtubule rescue by recruiting tubulin dimers to the microtubule

Jawdat Al-Bassam, Hwajin Kim, Gary Brouhard, Antoine van Oijen, Stephen C. Harrison, Fred Chang

Research output: Contribution to journalArticlepeer-review

130 Scopus citations


Spatial regulation of microtubule (MT) dynamics contributes to cell polarity and cell division. MT rescue, in which a MT stops shrinking and reinitiates growth, is the least understood aspect of MT dynamics. Cytoplasmic Linker Associated Proteins (CLASPs) are a conserved class of MT-associated proteins that contribute to MT stabilization and rescue in vivo. We show here that the Schizosaccharomyces pombe CLASP, Cls1p, is a homodimer that binds an αβ-tubulin heterodimer through conserved TOG-like domains. In vitro, CLASP increases MT rescue frequency, decreases MT catastrophe frequency, and moderately decreases MT disassembly rate. CLASP binds stably to the MT lattice, recruits tubulin, and locally promotes rescues. Mutations in the CLASP TOG domains demonstrate that tubulin binding is critical for its rescue activity. We propose a mechanism for rescue in which CLASP-tubulin dimer complexes bind along the MT lattice and reverse MT depolymerization with their bound tubulin dimer.

Original languageEnglish (US)
Pages (from-to)245-258
Number of pages14
JournalDevelopmental Cell
Issue number2
StatePublished - Aug 2010
Externally publishedYes



ASJC Scopus subject areas

  • Developmental Biology


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