PKD2L1 Membrane Protein Introduction

Introduction of PKD2L1

Polycystic kidney disease-2-like 1 (PKD2L1) is a member of the polycystin protein family consisting of PKD2 (polycystin-2), PKD2L1, and PKD2L2. PKD2L1 was first identified as a gene homologous to PKD2. Human PKD2L1 shows 50% amino acid sequence identity and 71% similarity with PKD2. PKD2L1 contains a putative Ca²⁺ binding EF hand motif and a predicted coiled-coil domain in its C-terminal cytoplasmic tail.

Basic Information of PKD2L1
Protein Name	Polycystic kidney disease 2-like 1 protein
Gene Name	PKD2L1
Aliases	Polycystin-2 homolog, Polycystin-2L1, Polycystin-L, Polycystin-L1
Organism	Homo sapiens (Human)
UniProt ID	Q9P0L9
Transmembrane Times	6
Length (aa)	805
Sequence	MNAVGSPEGQELQKLGSGAWDNPAYSGPPSPHGTLRVCTISSTGPLQPQPKKPEDEPQETAYRTQVSSCCLHICQGIRGLWGTTLTENTAENRELYIKTTLRELLVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDTGVSFQAISSMADFWDFAQGPLLDSLYWTKWYNNQSLGHGSHSFIYYENMLLGVPRLRQLKVRNDSCVVHEDFREDILSCYDVYSPDKEEQLPFGPFNGTAWTYHSQDELGGFSHWGRLTSYSGGGYYLDLPGSRQGSAEALRALQEGLWLDRGTRVVFIDFSVYNANINLFCVLRLVVEFPATGGAIPSWQIRTVKLIRYVSNWDFFIVGCEVIFCVFIFYYVVEEILELHIHRLRYLSSIWNILDLVVILLSIVAVGFHIFRTLEVNRLMGKLLQQPNTYADFEFLAFWQTQYNNMNAVNLFFAWIKIFKYISFNKTMTQLSSTLARCAKDILGFAVMFFIVFFAYAQLGYLLFGTQVENFSTFIKCIFTQFRIILGDFDYNAIDNANRILGPAYFVTYVFFVFFVLLNMFLAIINDTYSEVKEELAGQKDELQLSDLLKQGYNKTLLRLRLRKERVSDVQKVLQGGEQEIQFEDFTNTLRELGHAEHEITELTATFTKFDRDGNRILDEKEQEKMRQDLEEERVALNTEIEKLGRSIVSSPQGKSGPEAARAGGWVSGEEFYMLTRRVLQLETVLEGVVSQIDAVGSKLKMLERKGWLAPSPGVKEQAIWKHPQPAPAVTPDPWGVQGGQESEVPYKREEEALEERRLSRGEIPTLQRS

Function of PKD2L1 Membrane Protein

PKD2L1 is also believed to be a nonselective cation channel that can be regulated by voltage, protons, and calcium. It has been revealed that PKD2L1 is involved in the sour sensation and other pH-dependent processes. PKD2L1 has been shown to express in a discrete population of neurons surrounding the central canal of the spinal cord and may function to monitor the pH of the cerebrospinal fluid. In gustatory cells, pore-forming subunit of a channel formed by PKD1L2 and PKD1L3 contributes to sour taste perception.

Fig.1 Several models of sour taste detection. (Ishimaru, 2009)

Application of PKD2L1 Membrane Protein in Literature

Park E., et al. Identification of clustered phosphorylation sites in PKD2L1: how PKD2L1 channel activation is regulated by cyclic adenosine monophosphate signaling pathway. Pflugers Arch. 2018, 470(3):505-516. PubMed ID: 29230552

In this study, the authors observe the activity of PKD2L1 channel increased by the downstream cascades of β2AR and find the clustered phosphorylation sites, Ser-682, Ser-685, and Ser-686 that are significant in the channel regulation by phosphorylation.
Hussein S., et al. Acid-induced off-response of PKD2L1 channel in Xenopus oocytes and its regulation by Ca(2.). Scientific Reports. 2015, 5:15752. PubMed ID: 26502994

This study suggests that PKD2L1 may itself sense acids and defines off-response properties in the absence of PKD1L3.
Zheng W., et al. A novel PKD2L1 C-terminal domain critical for trimerization and channel function. Sci Rep. 2015, 5:9460. PubMed ID: 25820328

This study identifies C1 as the first PKD2L1 domain essential for both PKD2L1 trimerization and channel function, and suggests that PKD2L1 and PKD2L1/PKD1L3 channels share the PKD2L1 trimerization process.
Su Q., et al. Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1. Nat Commun. 2018, 9(1):1192. PubMed ID: 29567962

This study reveals the pore domain dilation is coupled to conformational changes of voltage-sensing domains (VSDs) via a series of π-π interactions, which suggests a potential PKD2L1 gating mechanism.
Shimizu T., et al. The asparagine 533 residue in the outer pore loop region of the mouse PKD2L1 channel is essential for its voltage-dependent inactivation. FEBS Open Bio. 2017, 7(9): 1392-1401. PubMed ID: 28904867

This report suggests that the N533 residue in the outer pore loop region of PKD2L1 plays an essential role in the voltage-dependent channel inactivation.

PKD2L1 Preparation Options

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Reference

Ishimaru Y and Matsunami H. (2009). Transient receptor potential (TRP) channels and taste sensation. Journal of Dental Research. 88(3): 212-218.

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