1997
DOI: 10.1038/ng0697-179
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Abstract: Autosomal dominant polycystic kidney disease (ADPKD) describes a group of at least three genetically distinct disorders with almost identical clinical features that collectively affects 1:1,000 of the population. Affected individuals typically develop large cystic kidneys and approximately one half develop end-stage renal disease by their seventh decade. It has been suggested that the diseases result from defects in interactive factors involved in a common pathway. The recent discovery of the genes for the two… Show more

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Cited by 620 publications
(511 citation statements)
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References 17 publications
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“…It is now accepted that PKD2 can function at the plasma membrane, but its activity there is under complex regulation involving shuttling between ER and plasma membrane, protein-protein interactions, and modes of activation. Specifically, it has been shown that the amount of PKD2 in the plasma membrane is dynamically regulated by interacting proteins (PKD1 [29,35], Polycystin-2 interactor, Golgi-and ER-associated protein-14 (PIGEA-14) [37]), posttranslational modifications (serine phosphorylation by casein kinase 2 (CK2) [38] and glycogen synthase kinase 3 (GSK3) [39]), interaction with other channel subunits in the plasma membrane (PKD1 [29,35,[40][41][42], TRPC1 [11], TRPV4 [43]) (Fig. 2), and finally, activation secondary to cell surface receptor activation (epidermal growth factor receptor (EGFR) [36]).…”
Section: Functional Compartmentalization Of Pkd2mentioning
confidence: 99%
“…It is now accepted that PKD2 can function at the plasma membrane, but its activity there is under complex regulation involving shuttling between ER and plasma membrane, protein-protein interactions, and modes of activation. Specifically, it has been shown that the amount of PKD2 in the plasma membrane is dynamically regulated by interacting proteins (PKD1 [29,35], Polycystin-2 interactor, Golgi-and ER-associated protein-14 (PIGEA-14) [37]), posttranslational modifications (serine phosphorylation by casein kinase 2 (CK2) [38] and glycogen synthase kinase 3 (GSK3) [39]), interaction with other channel subunits in the plasma membrane (PKD1 [29,35,[40][41][42], TRPC1 [11], TRPV4 [43]) (Fig. 2), and finally, activation secondary to cell surface receptor activation (epidermal growth factor receptor (EGFR) [36]).…”
Section: Functional Compartmentalization Of Pkd2mentioning
confidence: 99%
“…According to the current hypothesis, primary cilium is a kind of sensory organelle. Polycystin-1 and polycystin-2 co-localized in primary cilia forming PC complex through the C-terminal cytoplasmic tail domain [40]. PC1 exert the role of mechano/chemo-sensor, response to mechanical or fluid-induced cilia bending, and modulates Ca 2+ channel activity of polycystin-2, causing changes in intracellular Ca 2+ levels [48].…”
Section: Adpkd and Ciliamentioning
confidence: 99%
“…Polycystin-2 (968 amino acids) contains a short N-terminal cytoplasmic region with a ciliary targeting motif, 6 transmembrane domains, and a short C-terminal portion [38,39]. Polycystin-1 physically interacts with polycystin-2 through a coiled-coil domain in the C-terminal portion which forms the polycystin-signaling complex that play a role in chemosensory or mechanosensory signal transduction [40]. Disruption of both gene products results in similar clinical phenotypes.…”
Section: Introductionmentioning
confidence: 99%
“…The last six TM segments of PKD1 are homologous to PKD2 and other related TRP channels (45). PKD1 is not known to form a channel by itself but may complex with PKD2 to regulate its channel activity (46).…”
Section: The Trpp Subfamilymentioning
confidence: 99%