TRPML (transient receptor potential cation channel, mucolipin subfamily) comprises a group of three evolutionarily related proteins that belongs to the large family of
transient receptor potentialion channels. The three proteins
TRPML1,
TRPML2 and
TRPML3 are encoded by the mucolipin-1 (MCOLN1), mucolipin-2 (MCOLN2) and mucolipin-3 (MCOLN3) genes, respectively.
The three members of the TRPML ("ML" for mucolipin) sub-family are not extremely well characterized.[1]TRPML1 is known to be localized in late
endosomes.[2] This subunit also contains a lipase domain between its S1 and S2 segments. While the function of this domain is unknown it has been proposed that it is involved in channel regulation. Physiological studies have described TRPML1 channels as
proton leak channels in
lysosomes responsible for preventing these organelles from becoming too acidic.[2]TRPML2 and
TRPML3 more poorly characterized than
TRPML1.[3][4]
^
abColletti GA, Kiselyov K (January 2011). "Chapter 11: TRPML1". In Islam MS (ed.). Transient Receptor Potential Channels. Advances in Experimental Medicine and Biology. Vol. 704. Berlin: Springer. p. 700.
ISBN978-94-007-0264-6.
^Flores EN, García-Añoveros J (January 2011). "Chapter 12: TRPML2". In Islam MS (ed.). Transient Receptor Potential Channels. Advances in Experimental Medicine and Biology. Vol. 704. Berlin: Springer. p. 700.
ISBN978-94-007-0264-6.
^Noben-Trauth K (January 2011). "Chapter 13: TRPML3". In Islam MS (ed.). Transient Receptor Potential Channels. Advances in Experimental Medicine and Biology. Vol. 704. Berlin: Springer. p. 700.
ISBN978-94-007-0264-6.