Publication Date:
1986-04-18
Description:
The segregation of secretory proteins into the cisternae of the endoplasmic reticulum (ER) is normally tightly coupled to their synthesis. This feature distinguishes their biogenesis from that of proteins targeted to many other organelles. In the examples presented, translocation across the ER membrane is dissociated from translation. Transport, which is normally cotranslational, may proceed in the absence of chain elongation. Moreover, translocation across the ER membrane does not proceed spontaneously since, even in the absence of protein synthesis, energy substrates are required for translocation. These conclusions have been extended to the cotranslational integration of newly synthesized transmembrane proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perara, E -- Rothman, R E -- Lingappa, V R -- GM31626/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 18;232(4748):348-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3961485" target="_blank"〉PubMed〈/a〉
Keywords:
Biological Transport
;
Cell-Free System
;
Electrophoresis, Polyacrylamide Gel
;
Endoplasmic Reticulum/metabolism/physiology
;
Intracellular Membranes/metabolism/*physiology
;
Microsomes/metabolism
;
*Protein Biosynthesis
;
Proteins/*metabolism
;
RNA, Messenger/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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