Recombinant Human RABL5 protein

Supplementary information

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

RABL5 also known as RAB-like protein 5 is a member of the small GTPase superfamily. It weighs about 23 kDa and exhibits nucleotide-dependent switch activity similar to other Rab proteins. This protein is expressed in a variety of tissues with strong expression observed in the brain and reproductive organs. RABL5 plays roles in intracellular membrane trafficking and movement functioning as a molecular switch by cycling between active GTP-bound and inactive GDP-bound states.

Biological function summary

Research reveals important roles for RABL5 in vesicle movement and cellular communication. It functions as part of a larger complex involved in protein trafficking. It may work in concert with other small regulatory GTPases to modify signaling pathways. This protein assists in proper cellular distribution of proteins influencing processes such as growth and division and is especially relevant in cellular conditions that demand high energy or rapid turnover such as neural activities.

Pathways

There are two important biological contexts for RABL5. It influences the mTOR signaling pathway and the endocytosis pathway. In these pathways RABL5 seems to interact with proteins like RAB7 and RAB11. Its function in mTOR signaling is related to nutrient sensing and growth control while in endocytosis it contributes to managing vesicle trafficking and membrane recycling processes important for cellular homeostasis and communication.

Research connects RABL5 to neurodegenerative conditions and cancer. Dysregulation of this protein impacts synaptic function relevant to disorders like Alzheimer's disease where altered protein trafficking affects neuronal communication. Additionally abnormal regulation of the mTOR pathway by RABL5 can contribute to cancer as uncontrolled cell growth and division often result. The connection to these conditions highlights the importance of RABL5 interactions with proteins such as mTOR and factors involved in protein misfolding and synaptic dysfunction.