ArticleJournal of the American Society of Nephrology : JASN2008
The subcellular localization of TRPP2 modulates its function.
Article in Journal of the American Society of Nephrology : JASN, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Physiological functions and pharmacological targeting of transient receptor potential channels.Pharmacological reviews · 2025Review
- Review
- CaFaculty reviews · 2022Review
- An Overview of In Vivo and In Vitro Models for Autosomal Dominant Polycystic Kidney Disease: A Journey from 3D-Cysts to Mini-Pigs.International journal of molecular sciences · 2020Review
- Non-compaction of ventricular myocardium with polycystic kidney disease with cardiogenic cerebral embolism.BMJ case reports · 2020Article
- Identification and Expression Analysis of the Complete Family of ZebrafishFrontiers in cell and developmental biology · 2017Article
- New Insights into the Molecular Mechanisms Targeting Tubular Channels/Transporters in PKD Development.Kidney diseases (Basel, Switzerland) · 2016Review
- The functions of TRPP2 in the vascular system.Acta pharmacologica Sinica · 2016Review
- The zebrafish Kupffer's vesicle as a model system for the molecular mechanisms by which the lack of Polycystin-2 leads to stimulation of CFTR.Biology open · 2015Article
- Modulation of the secretory pathway rescues zebrafish polycystic kidney disease pathology.Journal of the American Society of Nephrology : JASN · 2014Article
- Cdc42 deficiency causes ciliary abnormalities and cystic kidneys.Journal of the American Society of Nephrology : JASN · 2013Article
- Polycystins and cellular Ca2+ signaling.Cellular and molecular life sciences : CMLS · 2013Review
- Polycystin-2 mutations lead to impaired calcium cycling in the heart and predispose to dilated cardiomyopathy.Journal of molecular and cellular cardiology · 2013Article
- Article
- Receptor protein tyrosine phosphatases are novel components of a polycystin complex.Biochimica et biophysica acta · 2011Article
- Zebrafish kidney development: basic science to translational research.Birth defects research. Part C, Embryo today : reviews · 2011Review
- A single amino acid residue constitutes the third dimerization domain essential for the assembly and function of the tetrameric polycystin-2 (TRPP2) channel.The Journal of biological chemistry · 2011Article
- The exocyst protein Sec10 interacts with Polycystin-2 and knockdown causes PKD-phenotypes.PLoS genetics · 2011Article
- Polycystin-2 activity is controlled by transcriptional coactivator with PDZ binding motif and PALS1-associated tight junction protein.The Journal of biological chemistry · 2010Article
- Down-regulation of Pkd2 by siRNAs suppresses cell-cell adhesion in the mouse melanoma cells.Molecular biology reports · 2010Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TRPP2, also known as polycystin-2, is a calcium permeable nonselective cation channel that is mutated in autosomal dominant polycystic kidney disease but has also been implicated in the regulation of cardiac development, renal tubular differentiation, and left-to-right (L-R) axis determination. For obtaining further insight into how TRPP2 exerts tissue-specific functions, this study took advantage of PACS-dependent trafficking of TRPP2 in zebrafish larvae. PACS proteins recognize an acidic cluster within the carboxy-terminal domain of TRPP2 that undergoes phosphorylation and mediate retrieval of TRPP2 to the Golgi and endoplasmic reticulum (ER). The interaction of human TRPP2 with PACS proteins can be inhibited by a Ser812Ala mutation (TRPP2(S812A)), thereby allowing TRPP2 to reach other subcellular compartments, and enhanced by a Ser812Asp mutation (TRPP2(S812D)), thereby trapping TRPP2 in the ER. It was found that the TRPP2(S812A) mutant rescued cyst formation of TRPP2-deficient zebrafish larvae to the same degree as wild-type TRPP2, whereas the TRPP2(S812D) mutant was significantly more effective in normalizing the distorted body axis of TRPP2-deficient fish. Surprisingly, the TRPP2(S812D) mutant rescued the abnormalities of L-R asymmetry more effectively than either wild-type or TRPP2(S812A), suggesting that the ER localization of TRPP2 plays an important role in the development of normal L-R asymmetry. Taken together, these findings support the hypothesis that TRPP2 assumes distinct subcellular localizations to exert tissue-specific functions.
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