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J. Biol. Chem., Vol. 277, Issue 37, 34042-34047, September 13, 2002
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From the Division of Molecular Medicine, Department of Medicine,
Columbia University, New York, New York 10032
Scavenger receptor B, type I (SR-BI) was recently
shown to interact with a PDZ domain-containing protein, PDZK1
(CLAMP/Diphor-1/CAP70/NaPi-Cap1), but the importance of this
interaction in vivo in terms of SR-BI function has not been
determined. In an effort to elucidate the role of this interaction
in vivo, the PDZK1-interacting domain of SR-BI was
identified and mutated and expressed liver-specifically in mice. The
PDZKI-interacting domain on SR-BI was identified as the last three
carboxyl-terminal amino acids, Arg-Lys-Leu. A mutant SR-BI
(SR-BIdel509) that lacked only the leucine in the PDZ-interacting
domain failed to interact with PDZK1 in vitro, while
showing normal selective uptake function in nonpolarized cells.
Transgenic mice with liver overexpression of SR-BIdel509 showed marked
accumulation of SR-BI mRNA with only a moderate increase in SR-BI
protein in liver, with no reduction in plasma cholesterol levels.
Measurement of cell surface SR-BI levels and HDL cholesteryl
ester-selective uptake in primary hepatocytes from transgenic mice
revealed that SR-BIdel509 was not expressed at the plasma membrane
correlating with normal levels of selective uptake compared with
hepatocytes from nontransgenic littermates. This study indicates that
the PDZK1-interacting domain of SR-BI is essential for cell surface
expression of SR-BI in liver and suggests that PDZK1 or other PDZ
domain proteins may play an important role in regulating SR-BI cell
surface expression and hence reverse cholesterol transport.
A Carboxyl-terminal PDZ-interacting Domain of Scavenger Receptor
B, Type I Is Essential for Cell Surface Expression in Liver*
*
This work was supported by American Heart Association
Scientist Development Grant AHA 0130305N (to D. L. S.) and
Pfizer International HDL Award Grant CU516105 (to D. L. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence may be addressed: Division of Molecular
Medicine, Dept. of Medicine, Columbia University, New York, NY 10032. Tel.: 212-305-5789; Fax: 212-305-5052; E-mail:
dls51@columbia.edu.
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