PC1 has been proposed to act as a
G protein–coupled receptor.[8][10] The C-terminal domain may be cleaved in a number of different ways. In one instance, a ~35 kDa portion of the tail has been found to accumulate in the
cell nucleus in response to decreased fluid flow in the mouse kidney.[11] In another instance, a 15 kDa fragment may be yielded, interacting with transcriptional activator and co-activator
STAT6 and
p100, or components of the canonical
Wnt signaling pathway in an inhibitory manner.[12][13]
The structure of the human PKD1-PKD2 complex has been solved by
cryo-electron microscopy, which showed a 1:3 ratio of PKD1 and PKD2 in the structure. PKD1 consists of a
voltage-gated ion channel fold that interacts with PKD2.[14]
Splice variants encoding different isoforms have been noted for PKD1. The gene is closely linked to six
pseudogenes in a known duplicated region on chromosome 16p.[16]
^Dalagiorgou G, Basdra EK, Papavassiliou AG (October 2010). "Polycystin-1: function as a mechanosensor". The International Journal of Biochemistry & Cell Biology. 42 (10): 1610–3.
doi:
10.1016/j.biocel.2010.06.017.
PMID20601082.
^Nauli SM, Alenghat FJ, Luo Y, Williams E, Vassilev P, Li X, Elia AE, Lu W, Brown EM, Quinn SJ, Ingber DE, Zhou J (February 2003). "Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells". Nature Genetics. 33 (2): 129–37.
doi:
10.1038/ng1076.
PMID12514735.
S2CID23149223.
PC1 has been proposed to act as a
G protein–coupled receptor.[8][10] The C-terminal domain may be cleaved in a number of different ways. In one instance, a ~35 kDa portion of the tail has been found to accumulate in the
cell nucleus in response to decreased fluid flow in the mouse kidney.[11] In another instance, a 15 kDa fragment may be yielded, interacting with transcriptional activator and co-activator
STAT6 and
p100, or components of the canonical
Wnt signaling pathway in an inhibitory manner.[12][13]
The structure of the human PKD1-PKD2 complex has been solved by
cryo-electron microscopy, which showed a 1:3 ratio of PKD1 and PKD2 in the structure. PKD1 consists of a
voltage-gated ion channel fold that interacts with PKD2.[14]
Splice variants encoding different isoforms have been noted for PKD1. The gene is closely linked to six
pseudogenes in a known duplicated region on chromosome 16p.[16]
^Dalagiorgou G, Basdra EK, Papavassiliou AG (October 2010). "Polycystin-1: function as a mechanosensor". The International Journal of Biochemistry & Cell Biology. 42 (10): 1610–3.
doi:
10.1016/j.biocel.2010.06.017.
PMID20601082.
^Nauli SM, Alenghat FJ, Luo Y, Williams E, Vassilev P, Li X, Elia AE, Lu W, Brown EM, Quinn SJ, Ingber DE, Zhou J (February 2003). "Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells". Nature Genetics. 33 (2): 129–37.
doi:
10.1038/ng1076.
PMID12514735.
S2CID23149223.