21 Facts About TRP channels

Transient receptor potential channels are a group of ion channels located mostly on the plasma membrane of numerous animal cell types.

Many of these TRP channels mediate a variety of sensations such as pain, temperature, different kinds of tastes, pressure, and vision.

TRP channels were initially discovered in the so-called "transient receptor potential" mutant strain of the fruit fly Drosophila, hence their name.

Later, TRP channels were found in vertebrates where they are ubiquitously expressed in many cell types and tissues.

Mammalian TRP channels are activated and regulated by a wide variety of stimuli and are expressed throughout the body.

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All of these sub-families are similar in that they are molecular sensing, non-selective cation TRP channels that have six transmembrane segments each sub-family is very unique and shares little structural homology with one another.

TRPA- or TRPA1-like channels exists in a variety of species as a phylogenetically distinct clade, but these are less well understood.

The phylogeny of TRPC channels has not been resolved in detail, but they are present across animal taxa.

Mutations in TRPC channels have been associated with respiratory diseases along with focal segmental glomerulosclerosis in the kidneys.

All TRPC channels are activated either by phospholipase C or diacyglycerol.

Mutations within TRPM channels have been associated with hypomagnesemia with secondary hypocalcemia.

TRPM channels have become known for their cold-sensing mechanisms, such is the case with TRPM8.

TRP channels are composed of 6 membrane-spanning helices with intracellular N- and C-termini.

Mammalian TRP channels are activated and regulated by a wide variety of stimuli including many post-transcriptional mechanisms like phosphorylation, G-protein receptor coupling, ligand-gating, and ubiquitination.

Each channel in this group is structurally unique, which adds to the diversity of functions that TRP channels possess there are some commonalities that distinguish this group from others.

TRP channels were initially discovered in the trp mutant strain of the fruit fly Drosophila which displayed transient elevation of potential in response to light stimuli and were so named transient receptor potential channels.

Importantly, many of these TRP channels mediate a variety of sensations like the sensations of pain, temperature, different kinds of tastes, pressure, and vision.

TRP ion channels convert energy into action potentials in somatosensory nociceptors.

Thermo-TRP channels have a C-terminal domain that is responsible for thermosensation and have a specific interchangeable region that allows them to sense temperature stimuli that is tied to ligand regulatory processes.

TRPM family of ion channels are particularly associated with prostate cancer where TRPM2, TRPM4, and TRPM8 are overexpressed in prostate cancer associated with more aggressive outcomes.

The identity of the mutated protein was unknown until it was cloned by Craig Montell, a post-doctoral researcher in Gerald Rubin's research group, in 1989, who noted its predicted structural relationship to TRP channels known at the time and Roger Hardie and Baruch Minke who provided evidence in 1992 that it is an ion channel that opens in response to light stimulation.