Differential localization of lipid phosphate phosphatases 1 and 3 to cell surface subdomains in polarized MDCK cells.
Lipid phosphate phosphatases (LPPs) are integral membrane proteins with six transmembrane domains that act as ecto-enzymes dephosphorylating a variety of extracellular lipid phosphates. Using polarized MDCK cells stably expressing human LPP1 and LPP3, we found that LPP1 was located exclusively at the apical surface whereas LPP3 was distributed mostly in the basolateral subdomain. We identified a novel apical sorting signal at the N-terminus of LPP1 composed of F(2)DKTRL(7). In the case of LPP3, a dityrosine motif present in the second cytoplasmic portion was identified as basolateral targeting signal. Our work shows that LPP1 and LPP3 are equipped with distinct sorting signals that cause them to differentially localize to the apical vs. the basolateral subdomain, respectively.
Jia
Yan-Jun
YJ
Department of Biochemistry, Sapporo Medical University School of Medicine, South-1, West-17, 060-8556 Sapporo, Japan.
Kai
Masahiro
M
Wada
Ikuo
I
Sakane
Fumio
F
Kanoh
Hideo
H
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology*; D016764:Cell Polarity; D004285:Dogs; D049452:Green Fluorescent Proteins; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008164:Luminescent Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010711:Phosphatidate Phosphatase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D021382:Protein Sorting Signals / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D007527:Isoenzymes; D008164:Luminescent Proteins; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; C112948:lipid phosphate phosphatase; D010711:Phosphatidate Phosphatase