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Prickle1 localized to the membrane through its farnesyl moiety, and the membrane localization was necessary for Prickle1 to regulate migration, to bind to CLASPs and LL5beta, and to promote microtubule targeting of focal adhesions.
catastrophe inhibition by SLAIN2 and CLASP1 supports mesenchymal cell shape in soft 3D matrices by enabling microtubules to perform a load-bearing function.
Acute silencing of CLASP1, a +TIP that participates in microtubule stabilization at the cell periphery, impairs trypomastigote internalization without diminishing the capacity for calcium-regulated lysosome exocytosis.
Propose that CLASPs couple microtubule organization, vesicle transport and cell interactions with the ECM, establishing a local secretion pathway that facilitates focal adhesion turnover by severing cell-matrix connections.
our data suggest a model for mitotic spindle positioning in which RanGTP and CLASP1 cooperate to align the spindle along the long axis of the dividing cell.
findings highlight the common mechanistic use of TOG domains in XMAP215 and CLASP families to regulate MT dynamics and suggest that differential TOG domain architecture may confer distinct functions to these critical cytoskeletal regulators
The epiblast epithelial status was maintained by anchoring microtubules to the basal cortex via CLIP1, a microtubule plus-end tracking protein, and Dystroglycan, a transmembrane protein that bridges the cytoskeleton and basement membrane (BM).
Data show that CENP-E-mediated traction forces on misaligned chromosomes are responsible for the irreversible loss of spindle-pole integrity in CLASP1/2-depleted cells.
Data show that the tau-related protein MAP4 and the microtubule rescue factor CLASP1 are essential for maintaining spindle position and the correct cell-division axis.
Data show that CLASP1-astrin-Kif2b complex acts as a central switch at kinetochores that defines mitotic progression and promotes fidelity by temporally regulating kinetochore-microtuble attachments.
These results suggest that CLASP1 is required at kinetochores to regulate the dynamic behavior of attached microtubules.
propose that CLASP1 and CLASP2 can mediate interactions between microtubule plus ends and the cell cortex and act as local rescue factors, possibly through forming a complex with EB1 at microtubule tips
A fusion protein of the putative microtubule-binding domain (1-662 out of 1289 residues) of hOrbit1 & GFP was transfected into human cells. The GFP-hOrbit1 N-terminal fragment binds to the newly formed microtubules rather than the pre-formed ones.
CLASPs provide apparent stabilization of microtubules by locally reducing the amplitude of growth/shortening episodes at the microtubule ends.
Data propose that PRC1 forms a link between stabilization of CLASP1 association with central spindle microtubules and anti-parallel microtubule elongation.
A role for microtubules that form at the Golgi membranes is identified in a manner dependent on the microtubule regulators CLASPs.
CLASPs, such as CLASP1, are nonmotor microtubule-associated proteins that interact with CLIPs (e.g., CLIP170\; MIM 179838). CLASP1 is involved in the regulation of microtubule dynamics at the kinetochore and throughout the spindle (Maiato et al., 2003
CLIP-associating protein 1-B
, Cytoplasmic linker-associated protein 1-B
, Protein Orbit homolog
, cytoplasmic linker associated protein 1
, CLIP-associating protein 1
, Cytoplasmic linker-associated protein 1
, CLIP-associating protein 1-like
, CLIP-associating protein CLASP1
, cytoplasmic linker-associated protein 1
, multiple asters 1
, multiple asters homolog 1
, protein Orbit homolog 1