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CLASP (show CLASRP Proteins) displays both plus end-binding and lattice-binding activities in nerve growth cones, and reveal that the two MT-binding activities regulate axon growth in an opposing manner
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 (show SLAIN2 Proteins) 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 (show MMRN1 Proteins), 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 (show CENPE Proteins)-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 (show MAP4 Proteins) and the microtubule rescue factor CLASP1 are essential for maintaining spindle position and the correct cell-division axis.
Data show that CLASP1-astrin (show SPAG5 Proteins)-Kif2b (show KIF2B Proteins) complex acts as a central switch at kinetochores that defines mitotic progression and promotes fidelity by temporally regulating kinetochore-microtuble attachments.
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