Anti-RABGAP1L/HHL antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

RABGAP1L also known as HHL is a GTPase-activating protein (GAP) that targets Rab GTPases which are important regulators of intracellular vesicle transport. The exact mass of the RABGAP1L protein is not well-documented but it is expressed in various tissues with significant presence in brain among others. This distribution suggests RABGAP1L's involvement in diverse cellular processes especially those requiring active vesicle trafficking and membrane dynamics.

Biological function summary

This protein acts as a regulatory molecule modulating the activity of Rab GTPases by accelerating the hydrolysis of GTP to GDP. This action helps switch the GTPases from an active to an inactive state which is vital for the spatial and temporal regulation of vesicular trafficking. RABGAP1L frequently associates with multiprotein complexes contributing to its regulatory functions in trafficking and signaling pathways.

Pathways

The protein plays a significant role in the endocytosis and exocytosis pathways that are vital for recycling membrane and macromolecules. RABGAP1L interacts with proteins like Rab11 in the endosomal recycling compartment which is essential for the efficient sorting and recycling of transmembrane proteins. These interactions highlight its involvement in the cellular management of vesicular transport and suggest its regulatory influence on several cellular processes.

Associated diseases and disorders

RABGAP1L links to conditions such as neurological disorders and cancer where dysregulation of vesicular trafficking is a common factor. For instance its interaction with proteins involved in synaptic vesicle trafficking possibly associates it with certain neurodegenerative disorders. It also relates with oncogenic processes through its influence on the transport pathways mirroring dysfunctions seen in other regulatory proteins involved in cancer pathways.