Mucolipin-1/MCOLN1 Protein, Human (Cell-Free, His)

TRPML1 Protein, a nonselective cation channel, is implicated in the regulation of membrane trafficking events and metal homeostasis. Extensively studied, it is proposed to play a crucial role in facilitating Ca(2+) release from late endosome and lysosome vesicles to the cytoplasm, thereby contributing to lysosome-dependent cellular processes such as organelle fusion, trafficking, exocytosis, and autophagy. TRPML1 is essential for efficient macrophage uptake of large particles, where lysosomal Ca(2+) release triggers lysosomal exocytosis and potentially influences phagosome-lysosome fusion. Additionally, it is involved in lactosylceramide trafficking, indicating a role in late endocytic membrane fusion/fission events. The channel's significance extends to the regulation of mTORC1 signaling and mTOR/TFEB-dependent lysosomal adaptation to environmental cues, including nutrient levels. Acting as a lysosomal active oxygen species (ROS) sensor, TRPML1 participates in ROS-induced TFEB activation and autophagy. Functioning as a Fe(2+) permeable channel in late endosomes and lysosomes, it also plays a role in zinc homeostasis, potentially interacting with TMEM163. In adaptive immunity, TRPML2 and TRPML1 may redundantly function in specialized lysosomes of B cells. Moreover, TRPML1's involvement in cellular lipase activity within the late endosomal pathway or at the cell surface suggests a role in membrane reshaping and vesiculation, particularly in the growth of tubular structures, although the direct conveyance of enzymatic activity remains unclear.