Sec13like

Sec13like refers to a family of proteins that are structurally and functionally related to the Saccharomyces cerevisiae Sec13 protein, a key component of the COPII coat complex involved in vesicle-mediated transport within the endoplasmic reticulum (ER) to the Golgi apparatus. The Sec13 protein is part of the Sec13/31p heterooctameric core, which assembles into the COPII coat, facilitating the formation of transport vesicles that carry newly synthesized proteins from the ER to the Golgi.

The Sec13like proteins are found across various eukaryotic organisms, including mammals, and share a conserved Sec13 domain, which is characterized by a β-propeller fold. This domain is essential for the protein’s role in vesicle formation and membrane curvature. While Sec13 itself is primarily involved in ER-to-Golgi transport, Sec13like proteins may participate in additional cellular processes, including intracellular trafficking, membrane remodeling, and potentially other vesicular transport pathways.

In humans, the Sec13like protein is encoded by the *SEC13L* gene. Studies suggest that it may play roles in maintaining cellular architecture and facilitating the assembly of multi-protein complexes involved in vesicle trafficking. Disruptions in Sec13like function have been linked to developmental abnormalities and cellular dysfunction, though its precise physiological roles remain an active area of research. The protein’s structural similarity to Sec13 implies overlapping mechanisms in vesicle formation, though its specific substrates and interacting partners may differ.

Beyond its role in vesicle trafficking, Sec13like proteins may also contribute to other cellular processes, such as cytoskeletal organization or signaling pathways. Research into Sec13like proteins continues to explore their broader functions, particularly in disease contexts, where alterations in vesicle-mediated transport can impact cellular homeostasis.