TRPV3 mutants causing <i>Olmsted Syndrome</i> induce impaired cell adhesion and nonfunctional lysosomes

Yadav, Manoj Kumar; Goswami, Chandan

doi:10.1080/19336950.2016.1249076

Cited by 21 publications

(20 citation statements)

References 37 publications

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“…Recently, some mutations in TRPV3: G573A, G573S, G573C and W692G have been detected leading to such disorders like Olmsted Syndrome (OS) [33,34] as well as other skin disorders [35]. These mutants were mainly retained in the ER [36] leading to reduced surface localization.…”

Section: Trpv3 Channel In Ermentioning

confidence: 99%

Role of the TRPV Channels in the Endoplasmic Reticulum Calcium Homeostasis

Haustrate

Prevarskaya

Lehen’kyi

2020

Cells

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It has been widely established that transient receptor potential vanilloid (TRPV) channels play a crucial role in calcium homeostasis in mammalian cells. Modulation of TRPV channels activity can modify their physiological function leading to some diseases and disorders like neurodegeneration, pain, cancer, skin disorders, etc. It should be noted that, despite TRPV channels importance, our knowledge of the TRPV channels functions in cells is mostly limited to their plasma membrane location. However, some TRPV channels were shown to be expressed in the endoplasmic reticulum where their modulation by activators and/or inhibitors was demonstrated to be crucial for intracellular signaling. In this review, we have intended to summarize the poorly studied roles and functions of these channels in the endoplasmic reticulum.

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Section: Trpv3 Channel In Ermentioning

confidence: 99%

Role of the TRPV Channels in the Endoplasmic Reticulum Calcium Homeostasis

Haustrate

Prevarskaya

Lehen’kyi

2020

Cells

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“…While being predicted to be an intracellular transmembrane protein by SURFY (score: 0.2954), SURFY2 predicted TRPV3 to be a surface-exposed transmembrane protein (score: 0.8383). Even though experimental subcellular localization data is still sparse for TRPV3, GFP-tagged TRPV3 expressed in a keratinocyte cell line has been shown to localize at the plasma membrane (29), substantially bolstering the prediction claim made by SURFY2. Here, the discrepant predictions could be explained by the absence of N-X-S/T glycosylation sites, the most relevant feature in SURFY, as well as the low non-cytoplasmic cysteine counts and absence of non-cytoplasmic C-glycosylation already encountered in the case of KCNT1.…”

Section: Investigating the Most Confident Re-classifications Of Transmentioning

confidence: 89%

Updating the in silico human surfaceome with meta-ensemble learning and feature engineering

Bojar

2018

Preprint

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Next to being targeted by most available drugs, human proteins located in the plasma membrane are also responsible for a plethora of essential cellular functions, ranging from signaling to transport processes. In order to target and study these transmembrane proteins, their plasma membrane location has to be established. Yet experimental validation of the thousands of potential plasma membrane proteins is laborious and technically challenging. A recent study performed machine learning to classify surface and non-surface transmembrane proteins in human cells based on curated high-quality training data from the Cell Surface Protein Atlas (CSPA) and other databases, reporting a cross-validation prediction accuracy of 93.5% (1). Here, we report an improved version of the surfaceome predictor SURFY, SURFY2, using the same training data with a meta-ensemble classification approach involving feature engineering. SURFY2 yielded predictions with an accuracy score of 95.5% on a test dataset never seen before by the classifier. Importantly, we found several high-confidence re-classifications of disease-relevant proteins among the discrepant predictions between SURFY and SURFY2. To rationalize the prediction mechanism of SURFY2 and analyze differently classified transmembrane proteins we investigated classifier feature importances and data distributions between prediction sets. SURFY2 exhibited both an increased precision as well as recall compared to SURFY and delivers the best in silico human surfaceome up to now. This updated version of the surfaceome will instigate further advances in drug targeting and research on cellular signaling as well as transport processes.

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“…Though initially it was assumed that all TRP channels are primarily localized in the plasma membrane, later reports have confirmed that different TRP channels have different yet specific distributions to subcellular membrane systems, including ER, Lysosome or endosome, where they participate complex tasks such as regulation of membrane trafficking signal transduction, maintenance of ion and pH homeostasis (Dong et al 2010;Yadav & Goswami. 2016).…”

Section: Presence Of Trp Channels In Mitochondriamentioning

confidence: 99%

TRPV4 interacts with mitochondrial proteins and acts as a mitochondrial structure-function regulator

Kumar

Majhi

Acharya

et al. 2018

Preprint

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TRPV4 has been linked with the development of sensory defects, neuropathic pain, neurodegenerative disorders such as Charcot Marie Tooth disease and various muscular dystrophies. In all these cases mitochondrial abnormalities were tagged as cellular hallmarks and such abnormalities have been reported as key factor for the pathophysiological conditions. Mitochondria also have the unique ability to sense and regulate their own temperature. Here, we demonstrate that TRPV4, a thermosensitive ion channels, localizes to a subpopulation of mitochondria in various cell lines, in primary cells and also in sperm cells. Improper expression and/or function of TRPV4 induce several mitochondrial abnormalities such as low oxidative potential, high Ca 2+ -influx and changes in electron transport chain functions. TRPV4 is also involved in regulation of mitochondrial morphology, smoothness, and fusion -fission events. The C-terminal cytoplasmic region of TRPV4 can localize it to mitochondria and interacts with mitochondrial proteins including Hsp60, Mfn1 and Mfn2. Regulation of mitochondria by TRPV4 may contribute to previously uncharacterized mitochondria-specific functions observed in various cell types. This discovery may help to link TRPV4-mediated channelopathies with mitochondria-mediated diseases.

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TRPV3 mutants causing Olmsted Syndrome induce impaired cell adhesion and nonfunctional lysosomes

Cited by 21 publications

References 37 publications

Role of the TRPV Channels in the Endoplasmic Reticulum Calcium Homeostasis

Role of the TRPV Channels in the Endoplasmic Reticulum Calcium Homeostasis

Updating the in silico human surfaceome with meta-ensemble learning and feature engineering

TRPV4 interacts with mitochondrial proteins and acts as a mitochondrial structure-function regulator

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