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¹ Skirball Institute of Biomolecular Medicine, School of Medicine, New York University, New York, NY 10016
² Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093

Correspondence to David Ron: ron{at}saturn.med.nyu.edu; or Randolph Y. Hampton: rhampton{at}ucsd.edu

Abstract
In addition to serving as the entry point for newly translated polypeptides making their way through the secretory pathway, the endoplasmic reticulum (ER) also synthesizes many lipid components of the entire endomembrane system. A report published in this issue implicates a signaling pathway known to respond to ER unfolded protein load in the control of phospholipid biosynthesis by the organelle (Sriburi et al., 2004). The reasonable notion that demand for ER membrane is integrated with protein processing capacity was initially suggested by genetic analysis of yeast. The new data lend direct support for this idea and imply interesting mechanistic possibilities for how this coupling develops.

Abbreviations used in this paper: UPR, unfolded protein response; XBP1, X-box binding protein 1.

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