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First published online November 9, 2005

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Arrestin' new details about LPA₁ internalization

Lysophosphatidic acid (LPA) evokes growth-factor-like responses in many cells through three related LPA receptors. Like many receptors, these can be internalized by endocytosis but the full details of their regulation are unclear. Harish Radhakrishna and colleagues now shed light on key aspects of this, in particular the involvement of cholesterol (see p. 5291). The authors show that both clathrin and the adaptor protein ß-arrestin are required for endocytosis of the LPA₁ receptor and that ß-arrestin, which targets many receptors to clathrin-coated pits, attenuates LPA signaling. In addition, they demonstrate that depletion of membrane cholesterol in HeLa cells inhibits LPA signalling, recruitment of ß-arrestin to the membrane, and the subsequent endocytosis of LPA₁. Finally, they show that LPA₁ localizes to cholesterol-rich microdomains upon ligand stimulation. These results provide new insights into the link between clathrin-mediated endocytic events and cholesterol-dependent processes at the plasma membrane. They also reveal an important aspect of the regulation of LPA₁, namely that cholesterol is required for its association with ß-arrestin prior to its clathrin-dependent endocytosis.

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Related articles in JCS:

A requirement for membrane cholesterol in the ß-arrestin- and clathrin-dependent endocytosis of LPA₁ lysophosphatidic acid receptors

Nikhil M. Urs, Kymry T. Jones, Paul D. Salo, Jamie E. Severin, JoAnn Trejo, and Harish Radhakrishna
JCS 2005 118: 5291-5304. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?