Membrane biogenesis and the unfolded protein response.
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.
Ron
David
D
Skirball Institute of Biomolecular Medicine, School of Medicine, New York University, New York, NY 10016, USA. ron@saturn.med.nyu.edu
Hampton
Randolph Y
RY
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D004722:Endoribonucleases; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism*; D050356:Lipid Metabolism; D008565:Membrane Proteins / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism; D017510:Protein Folding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D000071701:Regulatory Factor X Transcription Factors; D015398:Signal Transduction; D014157:Transcription Factors
D004268:DNA-Binding Proteins; D008565:Membrane Proteins; D009687:Nuclear Proteins; D000071701:Regulatory Factor X Transcription Factors; D014157:Transcription Factors; C403982:ERN2 protein, human; D017346:Protein Serine-Threonine Kinases; D004722:Endoribonucleases