Abstract
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 language | English (US) |
|---|---|
| Pages (from-to) | 245-258 |
| Number of pages | 14 |
| Journal | Developmental Cell |
| Volume | 19 |
| Issue number | 2 |
| DOIs | |
| State | Published - Aug 2010 |
| Externally published | Yes |
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Keywords
- CELLBIO
ASJC Scopus subject areas
- Developmental Biology
Cite this
CLASP promotes microtubule rescue by recruiting tubulin dimers to the microtubule. / Al-Bassam, Jawdat; Kim, Hwajin; Brouhard, Gary; van Oijen, Antoine; Harrison, Stephen C.; Chang, Fred.
In: Developmental Cell, Vol. 19, No. 2, 08.2010, p. 245-258.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - CLASP promotes microtubule rescue by recruiting tubulin dimers to the microtubule
AU - Al-Bassam, Jawdat
AU - Kim, Hwajin
AU - Brouhard, Gary
AU - van Oijen, Antoine
AU - Harrison, Stephen C.
AU - Chang, Fred
PY - 2010/8
Y1 - 2010/8
N2 - 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.
AB - 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.
KW - CELLBIO
UR - http://www.scopus.com/inward/record.url?scp=77955588492&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77955588492&partnerID=8YFLogxK
U2 - 10.1016/j.devcel.2010.07.016
DO - 10.1016/j.devcel.2010.07.016
M3 - Article
C2 - 20708587
AN - SCOPUS:77955588492
VL - 19
SP - 245
EP - 258
JO - Developmental Cell
JF - Developmental Cell
SN - 1534-5807
IS - 2
ER -