Rat Anti-CLASP2 Recombinant Antibody (KT69) (CBMAB-C3867WJ)

Cytoplasmic Linker Associated Protein 2

CLASP2 (Cytoplasmic Linker Associated Protein 2) is a Protein Coding gene. Diseases associated with CLASP2 include Clostridium Difficile Colitis. Among its related pathways are Signaling by Robo receptor and Developmental Biology. Gene Ontology (GO) annotations related to this gene include binding and microtubule plus-end binding. An important paralog of this gene is CLASP1.

Cytoplasmic Linker Associated Protein 2; Cytoplasmic Linker-Associated Protein 2; Protein Orbit Homolog 2; KIAA0627; HOrbit2;

Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921).

Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950).

This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514).

Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.

Cell division Source: UniProtKB-KW
Establishment of mitotic spindle localization Source: GO_Central
Establishment or maintenance of cell polarity Source: UniProtKB
Exit from mitosis Source: UniProtKB
Golgi organization Source: UniProtKB
Microtubule anchoring Source: UniProtKB
Microtubule cytoskeleton organization Source: UniProtKB
Microtubule nucleation Source: UniProtKB
Microtubule organizing center organization Source: UniProtKB
Mitotic spindle assembly Source: GO_Central
Mitotic spindle organization Source: UniProtKB
Negative regulation of focal adhesion assembly Source: UniProtKB
Negative regulation of microtubule depolymerization Source: UniProtKB
Negative regulation of stress fiber assembly Source: UniProtKB
Negative regulation of wound healing, spreading of epidermal cells Source: UniProtKB
Platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
Positive regulation of basement membrane assembly involved in embryonic body morphogenesis Source: UniProtKB
Positive regulation of epithelial cell migration Source: UniProtKB
Positive regulation of exocytosis Source: UniProtKB
Positive regulation of extracellular matrix disassembly Source: UniProtKB
Protein localization to plasma membrane Source: UniProtKB
Regulation of actin cytoskeleton organization Source: UniProtKB
Regulation of axon extension Source: UniProtKB
Regulation of epithelial to mesenchymal transition Source: UniProtKB
Regulation of gastrulation Source: UniProtKB
Regulation of microtubule-based process Source: UniProtKB
Regulation of microtubule polymerization Source: UniProtKB
Regulation of microtubule polymerization or depolymerization Source: UniProtKB
Vesicle targeting Source: UniProtKB

Cell membrane; Ruffle membrane; Cytoskeleton; Centrosome; Spindle; Golgi apparatus; Trans-Golgi network; Kinetochore. Localizes to microtubule plus ends (PubMed:15631994). Localizes to centrosomes, kinetochores and the mitotic spindle from prometaphase. Subsequently localizes to the spindle midzone from anaphase and to the midbody from telophase (PubMed:16866869, PubMed:16914514). In migrating cells localizes to the plus ends of microtubules within the cell body and to the entire microtubule lattice within the lamella. Localizes to the cell cortex and this requires ERC1 and PHLDB2 (PubMed:16824950). The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane.

Phosphorylated by GSK3B. Phosphorylation reduces MAPRE1 binding (PubMed:26003921). Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella.