Mechanism of Ca<sup>2+</sup>-dependent desensitization in TRP channels

Gordon‐Shaag, Ariela; Zagotta, William N.; Gordon, Sharona E.

doi:10.4161/chan.2.2.6026

Cited by 50 publications

(43 citation statements)

References 65 publications

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“…TRPM8 is, however, also produced in a range of tissues that are unlikely to be regulated by temperature, including sensory neurons (41) and the malignant prostate (42). The mechanism by which TRPM8 activity is regulated in these tissues remains to be fully determined; however, several regulatory mediators have been identified, including Ca 2+ , pH, PIP2 and phosphorylation (43)(44)(45)(46)(47). In those tissues where CRISP4 and TRPM8 are coexpressed (33), our data suggests that CRISP4 is also likely to modulate TRPM8 function.…”

Section: E)mentioning

confidence: 73%

Cysteine-rich secretory protein 4 is an inhibitor of transient receptor potential M8 with a role in establishing sperm function

Gibbs¹,

Orta

Reddy³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

100

110

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The cysteine-rich secretory proteins (CRISPs) are a group of four proteins in the mouse that are expressed abundantly in the male reproductive tract, and to a lesser extent in other tissues. Analysis of reptile CRISPs and mouse CRISP2 has shown that CRISPs can regulate cellular homeostasis via ion channels. With the exception of the ability of CRISP2 to regulate ryanodine receptors, the in vivo targets of mammalian CRISPs function are unknown. In this study, we have characterized the ion channel regulatory activity of epididymal CRISP4 using electrophysiology, cell assays, and mouse models. Through patch-clamping of testicular sperm, the CRISP4 CRISP domain was shown to inhibit the transient receptor potential (TRP) ion channel TRPM8. These data were confirmed using a stably transfected CHO cell line. TRPM8 is a major cold receptor in the body, but is found in other tissues, including the testis and on the tail and head of mouse and human sperm. Functional assays using sperm from wild-type mice showed that TRPM8 activation significantly reduced the number of sperm undergoing the progesteroneinduced acrosome reaction following capacitation, and that this response was reversed by the coaddition of CRISP4. In accordance, sperm from Crisp4 null mice had a compromised ability to undergo to the progesterone-induced acrosome reaction. Collectively, these data identify CRISP4 as an endogenous regulator of TRPM8 with a role in normal sperm function.cysteine-rich secretory proteins | antigen 5 | pathogenesis-related 1 | epididymal maturation | fertility

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Section: E)mentioning

confidence: 73%

Cysteine-rich secretory protein 4 is an inhibitor of transient receptor potential M8 with a role in establishing sperm function

Gibbs¹,

Orta

Reddy³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

100

110

View full text Add to dashboard Cite

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“…Although a sustained elevation of [Ca 2ϩ ] i is frequently observed in different types of TRPV4-positive cells (13,14,27,28), many TRP channels, including TRPV4, partially desensitize in patchclamp experiments (12,14,30). It has been reported that GSK1016790A can cause a rapid downregulation of TRPV4 within 3 min in TRPV4-transfected cells.…”

Section: Discussionmentioning

confidence: 99%

TRPV4 activation in mouse submandibular gland modulates Ca²⁺influx and salivation

Zhang

Catalán

Melvin

2012

American Journal of Physiology-Gastrointestinal and Liver Physi

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“…They can be activated or inhibited by Ca 2þ . Probably the earliest Ca 2þ -activated channel in phylogenies is the yeast mechanosensor TRPY1, in which Ca 2þ binds to clusters of negative charges in the C-terminus and greatly enhances the force-induced activation (Su et al 2009 ; and direct interaction with Ca 2þ /CaM (Nilius et al 2005b;Gordon-Shaag et al 2008;Nilius et al 2008). This interplay between Ca 2þ -dependent activation and inactivation provides a huge diversity of TRP-channel modulation in native cells.…”

Section: Trp Channels Depolarize Excitable Cells and Change Inwardly-mentioning

confidence: 99%

The Role of Transient Receptor Potential Cation Channels in Ca2+ Signaling

Gees

Colsoul²,

Nilius³

2010

Cold Spring Harbor Perspectives in Biology

382

361

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The 28 mammalian members of the super-family of transient receptor potential (TRP) channels are cation channels, mostly permeable to both monovalent and divalent cations, and can be subdivided into six main subfamilies: the TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPP ( polycystin), TRPML (mucolipin), and the TRPA (ankyrin) groups. TRP channels are widely expressed in a large number of different tissues and cell types, and their biological roles appear to be equally diverse. In general, considered as polymodal cell sensors, they play a much more diverse role than anticipated. Functionally, TRP channels, when activated, cause cell depolarization, which may trigger a plethora of voltage-dependent ion channels. Upon stimulation, Ca 2þ permeable TRP channels generate changes in the intracellular Ca 2þ concentration, [Ca 2þ ] i , by Ca 2þ entry via the plasma membrane. However, more and more evidence is arising that TRP channels are also located in intracellular organelles and serve as intracellular Ca 2þ release channels. This review focuses on three major tasks of TRP channels: (1) the function of TRP channels as Ca 2þ entry channels; (2) the electrogenic actions of TRPs; and (3) TRPs as Ca 2þ release channels in intracellular organelles.T ransient receptor potential (TRP) channels constitute a large and functionally versatile family of cation-conducting channel proteins, which have been mainly considered as polymodal unique cell sensors. The first TRP channel gene was discovered in Drosophila melanogaster (Montell and Rubin 1989) in the analysis of a mutant fly whose photoreceptors failed to retain a sustained response to maintained light stimuli. So far, more than 50 TRP channels have been identified with representative members in many species. The evolutionary first TRP channels in protists, chlorophyte algae, choanoflagellates, yeast, and fungi are primary chemo-, thermo-, or mechanosensors (Cai 2008;Wheeler and Brownlee 2008;Chang et al. 2010;Matsuura et al. 2009). Many of these functions are remarkably conserved from protists, worms, and flies to humans (Montell 2005;Pedersen et al. 2005;Nilius et al. 2007;Damann et al. 2008). More than 50 trp genes have been cloned so far that comprise approximately 20% of the known genes encoding ion channels. In mammals, 28 TRP channels were found and classified according to homology into 6 subfamilies: TRPC (canonical), TRPV (vanilloid),

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Mechanism of Ca²⁺-dependent desensitization in TRP channels

Cited by 50 publications

References 65 publications

Cysteine-rich secretory protein 4 is an inhibitor of transient receptor potential M8 with a role in establishing sperm function

Cysteine-rich secretory protein 4 is an inhibitor of transient receptor potential M8 with a role in establishing sperm function

TRPV4 activation in mouse submandibular gland modulates Ca²⁺influx and salivation

The Role of Transient Receptor Potential Cation Channels in Ca2+ Signaling

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Mechanism of Ca2+-dependent desensitization in TRP channels

Cited by 50 publications

References 65 publications

Cysteine-rich secretory protein 4 is an inhibitor of transient receptor potential M8 with a role in establishing sperm function

Cysteine-rich secretory protein 4 is an inhibitor of transient receptor potential M8 with a role in establishing sperm function

TRPV4 activation in mouse submandibular gland modulates Ca2+influx and salivation

The Role of Transient Receptor Potential Cation Channels in Ca2+ Signaling

Contact Info

Product

Resources

About

Mechanism of Ca²⁺-dependent desensitization in TRP channels

TRPV4 activation in mouse submandibular gland modulates Ca²⁺influx and salivation