Tubulin Folding Cofactor E Like Protein (TBCEL)

LRRC35 did not play a role in tubulin heterodimer assembly and had no effect on the tubulin GTPase activity of cofactor C (TBCC) and cofactor D (TBCD). Overexpression of LRRC35 caused microtubule destruction by disrupting tubulin heterodimers and targeting tubulin to the proteasome for degradation. cells depleted of LRRC35 retained stable microtubules, mostly concentrated in the perinuclear region, and displayed a clustering of endoplasmic reticulum, Golgi, and lysosomal organelle membranes in a condensed region of the cytoplasm. LRRC35 regulation of microtubule network stability affects vesicle trafficking mediated by microtubule-dependent molecular motors.The deduced 425-amino acid protein shares 23% amino acid identity with TBCE and contains a leucine-rich repeat followed by a ubiquitin-like motif.