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Role of phosphorylation of the cytoplasmic domain of the alpha(2)-macroglobulin receptor (LRP).

Abstract：

:The low density lipoprotein receptor-related protein (alpha(2)MR/LRP) is a cell surface receptor which is present on most cells and tissues. We show that the 85 kDa subunit, containing the transmembrane region and cytoplasmic domain is phosphorylated in vivo. Comparison of the phosphorylation of the low density lipoprotein receptor (LDLR) with a chimeric receptor containing the cytoplasmic domain of the alpha(2)MR/LRP (LDLR/LRP) showed that phosphorylation is exclusive to the cytoplasmic domain. Staurosporine, a general kinase inhibitor, resulted in a 40% lowering of phosphorylation of LDLR/LRP, but did not give rise to measurable changes in its membrane traffic in MDCK cells. The role of phosphorylation on degradation of the receptor was studied using inhibitors of lysosomal and proteasomal degradation. These studies showed that LDLR/LRP was rapidly turned over by proteasomal degradation but that this turnover was also not a consequence of phosphorylation.

journal_name

Cell Biol Int

journal_title

Cell biology international

authors

Djordjevic JT,Waterkeyn JG,Hennessy KL,Stanley KK

doi

10.1006/cbir.2000.0561

keywords:

subject

Has Abstract

pub_date

2000-01-01 00:00:00

pages

599-610

issue

9

eissn

1065-6995

issn

1095-8355

pii

S1065-6995(00)90561-4

journal_volume

24

pub_type

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