Targeting of proteins into the eukaryotic secretory pathway: signal peptide structure/function relationships.
Much progress has been made in recent years regarding the mechanisms of targeting of secretory proteins to, and across, the endoplasmic reticulum (ER) membrane. Many of the cellular components involved in mediating translocation across this bilayer have been identified and characterized. Polypeptide domains of secretory proteins, termed signal peptides, have been shown to be necessary, and in most cases sufficient, for entry of preproteins into the lumen of the ER. These NH2-terminal segments appear to serve multiple roles in targeting and translocation. The structural features which mediate their multiple functions are currently the subject of intense study.
Nothwehr
S F
SF
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri, 63110.
Gordon
J I
JI
D000818:Animals; D004721:Endoplasmic Reticulum / Q000502:physiology; D011498:Protein Precursors / Q000502:physiology; D021382:Protein Sorting Signals / Q000502:physiology*; D011506:Proteins / Q000378:metabolism*; D013329:Structure-Activity Relationship
D011498:Protein Precursors; D021382:Protein Sorting Signals; D011506:Proteins