Microtubule crosslinking factor 1 (MTCL1)

Microtubule crosslinking factor 1 (MTCL1) is a large, coiled-coil cytoskeletal protein that plays a dual role in directly crosslinking and stabilizing microtubules in non-centrosomal arrays, such as those found around the Golgi apparatus and in polarized epithelial cells[1][3]. MTCL1 acts as a dimer and possesses two distinct microtubule-binding domains: the N-terminal domain crosslinks microtubules without affecting dynamics, while the C-terminal domain stabilizes microtubules and facilitates bundled microtubule assemblies[1][3]. MTCL1 is essential for the formation and maintenance of the perinuclear microtubule network that supports Golgi ribbon morphology, and is critical for the structural integrity of Purkinje neuron axons and apico-basal polarity in epithelial cells[1][3][4]. Currently, MTCL1 is not a recognized therapeutic target, and there are no known drugs or drug mechanisms that specifically target this protein.

Other names

CCDC165KIAA0802SOGA2Coiled-coil domain-containing protein 165PAR-1-interacting proteinSOGA family member 2