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Journal of Biochemistry Advance Access originally published online on September 27, 2006
Journal of Biochemistry 2006 140(5):677-686; doi:10.1093/jb/mvj195
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© 2006 The Japanese Biochemical Society.

ARTICLE

Lipid Phosphate Phosphatases 1 and 3 Are Localized in Distinct Lipid Rafts

Masahiro Kai, Fumio Sakane, Yan-Jun Jia, Shin-ichi Imai, Satoshi Yasuda and Hideo Kanoh*

Department of Biochemistry, Sapporo Medical University School of Medicine, West-17, South-1, Sapporo 060-8556

* To whom correspondence should be addressed. Tel: +81-11-611-2111, Fax: +81-11-622-1918, E-mail: kanoh{at}sapmed.ac.jp

Lipid phosphate phosphatases (LPPs), integral membrane proteins with six transmembrane domains, dephosphorylate a variety of extracellular lipid phosphates. Although LPP3 is already known to bind to Triton X-100–insoluble rafts, we here report that LPP1 is also associated with lipid rafts distinct from those harboring LPP3. We found that LPP1 was Triton X-100–soluble, but CHAPS-insoluble in LNCaP cells endogenously expressing LPP1 and several LPP1 cDNA–transfected cells including NIH3T3 fibroblasts. In addition to the non–ionic detergent insolubility, LPP1 further possessed several properties formulated for raft-localizing proteins as follows: first, the CHAPS-insolubility was resistant to the actin-disrupting drug cytochalasin D; second, the CHAPS-insoluble LPP1 floated in an Optiprep density gradient; third, the CHAPS insolubility of LPP1 was lost by cholesterol depletion; and finally, the subcellular distribution pattern of LPP1 exclusively overlapped with that of a raft marker, cholera toxin B subunit. Interestingly, confocal microscopic analysis showed that LPP1 was distributed to membrane compartments distinct from those of LPP3. Analysis using various LPP1/LPP3 chimeras revealed that their first extracellular regions determine the different Triton X-100 solubilities. These results indicate that LPP1 and LPP3 are distributed in distinct lipid rafts that may provide unique microenvironments defining their non-redundant physiological functions.


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