327:, tetrapropylammonium, tetrapentenyl ammonium). The channel diameter was estimated to be at least 1.1 Å. Both are reported to be integral membrane proteins with 7-11 TMSs (PKD1) and 6 TMSs (PKD2), respectively. They share a homologous region of about 400 residues (residues 206-623 in PKD2; residues 3656-4052 in PKD1) which includes five TMSs of both proteins. This may well be the channel domain. PKD2 and polycystin-L have been shown to exhibit voltage-, pH- and divalent cation-dependent channel activity. PKD1 may function primarily in regulation, both activating and stabilizing the polycystin-2 channel.
336:
left-right asymmetry development. TRPP3 is implicated in sour tasting in bipolar cells of taste buds of the tongue and in the regulation of pH-sensitive action potential in neurons surrounding the central canal of the spinal cord. TRPP3 is present in both excitable and non-excitable cells in various tissues, such as retina, brain, heart, testis, and kidney.
374:
Autosomal recessive polycystic kidney disease is caused by mutations in PKHD1, which encodes the membrane-associated receptor-like protein fibrocystin/polyductin (FPC) (Q8TCZ9, 4074aaa). FPC associates with the primary cilia of epithelial cells and co-localizes with the Pkd2 gene product polycystin-2
310:
Polycystin-L has been shown to be a cation (Na, K and Ca) channel that is activated by Ca, while polycystin-2 has been characterized as a Ca-permeable cation-selective channel. Two members of the PCC family (polycystin 1 and 2; PKD1 and 2) are mutated in human autosomal dominant polycystic kidney
335:
Transient receptor potential (TRP) polycystin 2 and 3 (TRPP2 and 3) are homologous members of the TRP superfamily of cation channels but have different physiological functions. TRPP2 is part of a flow sensor, and is defective in autosomal dominant polycystic kidney disease and implicated in
361:
Alpha-actinin is an actin-bundling protein known to regulate several types of ion channels. Planer lipid bilayer electrophysiology showed that TRPP3 exhibits cation channel activities that are substantially augmented by alpha-actinin. The TRPP3-alpha-actinin association was documented by
285:
imaging has revealed the domain structure of polycystin-1. It exhibits minimal sequence similarities, but similar domain organization and membrane topology with established cation channels such as the transient receptor potential (TRP) and voltage-gated ion channel (VIC) family proteins
344:
The TRP-ML1 protein (Mucolipin-1) has been shown to be a lysosomal monovalent cation channel that undergoes inactivating proteolytic cleavage. It shows greater sequence similarity to the transmembrane region of polycystin 2 than it does to members of the TRP-CC family
927:
298:, leads to development of ADPKD (autosomal-dominant polycystic kidney disease). Besides modulating channel activity and related signaling events, the CRDs (C-terminal regulatory domains) of PKD2 and PKD2L1 play a central role in channel
280:
description, polycystin 1 contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. However,
527:
Molland KL, Narayanan A, Burgner JW, Yernool DA (July 2010). "Identification of the structural motif responsible for trimeric assembly of the C-terminal regulatory domains of polycystin channels PKD2L1 and PKD2".
172:) consists of several transporters ranging in size from 500 to over 4000 amino acyl residues (aas) in length and exhibiting between 5 and 18 transmembrane segments (TMSs). This family is a constituent of the
294:, respectively). However, PSI-BLAST without iterations does not pick up these similarities. The PKD2L1-PKD1L3 complex perceives sour taste. Disruption of the PKD2-PKD1 complex, responsible for
311:
disease, and polycystin-L, very similar and probably orthologous to PKD2, is deleted in mice with renal and retinal defects. PKD1 and 2 interact to form the non-selective cation channel
931:
132:
88:
76:
276:
Human polycystin 1 is a huge protein of 4303 amino acyl residues (aas). Its repeated leucine-rich (LRR) segment is found in many proteins. According to the
176:. These transporters generally catalyze the export of cations. A representative list of proteins belonging to the PCC family can be found in the
752:
457:
Oatley P, Stewart AP, Sandford R, Edwardson JM (April 2012). "Atomic force microscopy imaging reveals the domain structure of polycystin-1".
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where it associates with alpha-actinin-2. Alpha-actinin attaches TRPP3 to the cytoskeleton and up-regulates its channel function.
315:
but PKD2 can form channels in the absence of any other associated protein. Polycystin-2 transports a variety of organic cations (
957:
869:
Kim I, Fu Y, Hui K, Moeckel G, Mai W, Li C, Liang D, Zhao P, Ma J, Chen XZ, George AL, Coffey RJ, Feng ZP, Wu G (March 2008).
604:
Gonzalez-Perrett S, Batelli M, Kim K, Essafi M, Timpanaro G, Moltabetti N, Reisin IL, Arnaout MA, Cantiello HF (July 2002).
152:
362:
co-immunoprecipitation using native cells and tissues, yeast two-hybrid, and in vitro binding assays. TRPP3 is abundant in
375:(PC2). Kim et al. (2008) have concluded that a functional and molecular interaction exists between FPC and PC2 in vivo.
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384:
350:
173:
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Kiselyov K, Chen J, Rbaibi Y, Oberdick D, Tjon-Kon-Sang S, Shcheynikov N, Muallem S, Soyombo A (December 2005).
140:
871:"Fibrocystin/polyductin modulates renal tubular formation by regulating polycystin-2 expression and function"
282:
694:
Xu GM, González-Perrett S, Essafi M, Timpanaro GA, Montalbetti N, Arnaout MA, Cantiello HF (January 2003).
188:
There are a number of crystal structures available for members of the PCC family. Some of these include:
492:
Dalagiorgou G, Basdra EK, Papavassiliou AG (October 2010). "Polycystin-1: function as a mechanosensor".
349:). Therefore, it is included in the former family. Both the PCC and TRP-CC families are members of the
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606:"Voltage dependence and pH regulation of human polycystin-2-mediated cation channel activity"
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Li Q, Dai XQ, Shen PY, Wu Y, Long W, Chen CX, Hussain Z, Wang S, Chen XZ (December 2007).
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830:"TRP-ML1 is a lysosomal monovalent cation channel that undergoes proteolytic cleavage"
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739:. Advances in Experimental Medicine and Biology. Vol. 704. pp. 229–37.
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Noben-Trauth K (1 January 2011). "The TRPML3 Channel: From Gene to
Function".
647:"Modulation of the human polycystin-L channel by voltage and divalent cations"
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Liu Y, Li Q, Tan M, Zhang YY, Karpinski E, Zhou J, Chen XZ (August 2002).
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565:"Organic cation permeation through the channel formed by polycystin-2"
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Group of membrane proteins that passively export cations out of a cell
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781:"Direct binding of alpha-actinin enhances TRPP3 channel activity"
696:"Polycystin-1 activates and stabilizes the polycystin-2 channel"
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Creative
Commons Attribution-ShareAlike 3.0 Unported License
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926:, which is licensed in a way that permits reuse under the
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923:"1.A.5 The Polycystin Cation Channel (PCC) Family"
415:"1.A.5 The Polycystin Cation Channel (PCC) Family"
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875:Journal of the American Society of Nephrology
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204:Polycystic kidney disease 2-like 1 protein:
174:Voltage-Gated Ion Channel (VIC) Superfamily
22:C-terminal Cytosolic Domain of Polycystin-2
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302:. These proteins appear to form trimers.
563:Anyatonwu GI, Ehrlich BE (August 2005).
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934:. All relevant terms must be followed.
166:Polycystin Cation Channel (PCC) Family
18:
737:Transient Receptor Potential Channels
331:Transient receptor potential proteins
7:
834:The Journal of Biological Chemistry
700:The Journal of Biological Chemistry
610:The Journal of Biological Chemistry
569:The Journal of Biological Chemistry
395:Transporter Classification Database
178:Transporter Classification Database
14:
920:, this article uses content from
798:10.1111/j.1471-4159.2007.04940.x
1:
664:10.1016/s0014-5793(02)03071-5
104:Available protein structures:
745:10.1007/978-94-007-0265-3_13
506:10.1016/j.biocel.2010.06.017
989:
973:Integral membrane proteins
963:Transmembrane transporters
370:Physiological significance
785:Journal of Neurochemistry
385:Voltage-gated ion channel
99:
530:The Biochemical Journal
283:atomic force microscopy
958:Transmembrane proteins
887:10.1681/ASN.2007070770
847:10.1074/jbc.M508210200
713:10.1074/jbc.M209996200
623:10.1074/jbc.M105084200
582:10.1074/jbc.M504359200
930:, but not under the
440:"P98161-PKD1 Human"
968:Transport proteins
542:10.1042/BJ20091843
325:tetrabutylammonium
321:tetraethylammonium
184:Crystal Structures
953:Membrane proteins
754:978-94-007-0264-6
471:10.1021/bi300134b
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153:structure summary
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948:Protein families
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306:Polycystin-L
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390:Ion channel
364:mouse brain
340:Mucolipin-1
89:OPM protein
27:Identifiers
942:Categories
401:References
267:Homologues
116:structures
918:this edit
347:TC# 1.A.4
313:in vitro,
292:TC# 1.A.1
288:TC# 1.A.4
257:,
251:,
245:,
239:,
233:,
214:,
170:TC# 1.A.5
58:IPR013122
905:18235088
856:16257972
815:84357640
807:17944866
763:21290299
722:12407099
673:12163164
632:11991947
591:15961385
550:20408813
514:20601082
479:22409330
424:10 April
379:See also
263:
220:
201:
133:RCSB PDB
53:InterPro
896:2391052
681:3150744
444:Uniprot
278:UniProt
46:PF08016
916:As of
903:
893:
854:
813:
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512:
477:
223:PKD2:
191:PKD1:
148:PDBsum
122:
112:
32:Symbol
811:S2CID
677:S2CID
70:1.A.5
932:GFDL
901:PMID
852:PMID
803:PMID
759:PMID
749:ISBN
718:PMID
669:PMID
628:PMID
587:PMID
546:PMID
510:PMID
475:PMID
426:2016
419:TCDB
290:and
260:2Y4Q
254:2KQ6
248:3HRO
242:3HRN
236:2KLE
230:2KLD
217:4GIF
211:3TE3
198:1B4R
164:The
141:PDBj
137:PDBe
120:ECOD
110:Pfam
94:5mkf
65:TCDB
41:Pfam
35:PKD2
891:PMC
883:doi
842:doi
838:280
793:doi
789:103
741:doi
708:doi
704:278
659:doi
655:525
618:doi
614:277
577:doi
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538:doi
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502:doi
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226:PDB
207:PDB
194:PDB
128:PDB
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Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.