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PKD2L1 encodes a member of the polycystin protein family. Additionally we are shipping PKD2L1 Antibodies (34) and many more products for this protein.
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sour taste cells in the posterior tongue express a proton current; the current is present in PKD2L1-expressing taste cells from circumvallate, foliate, and fungiform papillae but not in a variety of other cells
findings suggest that PKD2L1 partly contributes to sour taste responses in mice and that receptors other than PKDs would be involved in sour detection
All channel-forming isoforms of TRPP channels (polycystin-2 (show PKD2 Proteins), polycystin-L, and polycystin-2L2 (show PKD2L2 Proteins)) were expressed in adult mouse lacrimal gland.
These results demonstrate that Asp (show C3 Proteins)(523) in PKD2L1 is a key determinant of Ca(2 (show CA2 Proteins)+) permeation into the PKD1L3 (show PKD1L3 Proteins)/PKD2L1 complex and that PKD2L1 contributes to forming the pore of the PKD1L3 (show PKD1L3 Proteins)/PKD2L1 channel.
the PKD2L1-PKD1L3 (show PKD1L3 Proteins) complex is involved in acid sensing in vivo
PKD2L1 forms functional cation channels on the plasma membrane by interacting with PKD1 (show PKD1 Proteins)
Pkd1l3 (show PKD1L3 Proteins) and Pkd2l1 are co-expressed in a select subset of taste receptor cells and therefore may, like other PKD (show PRKD1 Proteins) channels, function as a heteromer.
These results suggest that PKD1L3 (show PKD1L3 Proteins) and PKD2L1 heteromers may function as sour taste receptors.
Animals lacking PKD2L1-expressing cells are completely devoid of taste responses to sour stimuli.
The taste receptor PKD2L1 is expressed by type III taste cells, but not by type I and II cells, in the mouse taste bud.
our study identified C1 as the first PKD2L1 domain essential for both PKD2L1 trimerization and channel function, and suggest that PKD2L1 and PKD2L1/PKD1L3 (show PKD1L3 Proteins) channels share the PKD2L1 trimerization process.
Trimerization may be important for both homo- and possibly heteromeric assemblies of PKD2L1.
This study demonistrated that human PKD2L play the role of food preference behavior.
Pkd2L1 is a novel target channel whose function is regulated by the versatile scaffolding protein RACK1 (show GNB2L1 Proteins).
Despite the moderate sequence identity between C-terminal regulatory domains (CRDs) of PKD2 (show PKD2 Proteins) and PKD2L1, they both form trimers, implying that trimeric organization of CRDs may be true of all polycystin channels.
The calcium-binding EF-hand in polycystin-L is not a domain for channel activation and ensuing inactivation.
Taken together, alpha-actinin (show ACTN1 Proteins) not only attaches TRPP3 to the cytoskeleton but also up-regulates TRPP3 channel function.
This gene encodes a member of the polycystin protein family. The encoded protein contains multiple transmembrane domains, and cytoplasmic N- and C-termini. The protein may be an integral membrane protein involved in cell-cell/matrix interactions. This protein functions as a calcium-regulated nonselective cation channel. Two transcript variants encoding different isoforms have been found for this gene.
polycystic kidney disease 2-like 1
, polycystic kidney disease 2-like 1 protein-like
, polycystic kidney disease 2-like 1 protein
, polycystin-2 homolog
, transient receptor potential cation channel, subfamily P, member 3