TBC1 domain family member 14 (TBC1D14)

TBC1 domain family member 14 (TBC1D14) is a cytoplasmic protein characterized by a C-terminal TBC (Tre2-Bub2-Cdc16) domain typical for Rab GTPase-activating proteins (RabGAPs), although TBC1D14 does not exhibit classical RabGAP enzymatic activity. Its primary biological role is as a negative regulator of autophagy: TBC1D14 controls the delivery of membranes from RAB11-positive recycling endosomes to forming autophagosomes. It functions by interacting with the TRAPP complex—specifically with the TRAPPIII-like complex through the TRAPPC8 subunit—and modulating trafficking of ATG9, which is essential for autophagosome formation. Overexpression of TBC1D14 perturbs autophagy initiation and secretory trafficking. While it binds RAB11 and has features of a Rab effector, it does not act as a GAP for RAB11. TBC1D14 is localized to the Golgi, autophagosome, and recycling endosome. Currently, TBC1D14 is not categorized as a classical therapeutic target such as a receptor, enzyme, transporter, or ion channel[1][2][3].

Other names

TBC1D14KIAA1322TBC1 domain family member 14