Family

Transient receptor potential channel, vanilloid 4 (IPR008348)

Short name: TRPV4_channel

Family relationships

Description

TRP (transient receptor potential) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [PMID: 18535090].

TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies [PMID: 20025796]: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin), whose only member is the transmembrane protein 1, TRPP(polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogenous properties and complex regulation.

TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [PMID: 20861159].

The TRPV (vanilloid) subfamily can be divided into two distinct groups. The first, which comprises TRPV1, TRPV2, TRPV3, and TRPV4, has members which can be activated by temperature as well as chemical stimuli. They are involved in a range of functions including nociception, thermosensing and osmolarity sensing. The second group, which consists of TRPV5 and TRPV6, (also known as epithelial calcium channels 1 and 2) are involved in renal Ca2+ absorption/reabsorption [PMID: 19297520].

TRPV4 is expressed at high levels in the kidney, liver, heart and central nervous system. It is activated by extracellular hypo-osmoticity, leading to increased transcellular ion flux and paracellular permeability, which may allow the cells to adjust to changes in extracellular osmolarity [PMID: 17233610, PMID: 11081638]. TRPV4 is can also be activated chemically by metabolites of arachidonic acid and alpha-isomers of phorbol esters [PMID: 11827975]. Heat activation has also been detected, though its extent appears to be dependent on the degree of hypo-osmoticity [PMID: 12151520].

GO terms

Biological Process

GO:0006811 ion transport

Molecular Function

GO:0005216 ion channel activity

Cellular Component

GO:0016021 integral component of membrane

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PRINTS
PANTHER