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Article:Endoplasmic reticulum
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m (Reverted edits by 217.158.134.45 (talk) to last version by Microtubules)
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The quantity of RER and SER in a cell can slowly interchange from one type to the other, depending on changing metabolic needs. Transformation can include embedment of new proteins in membrane as well as structural changes. Massive changes may also occur in protein content without noticeable structural changes.
 
The quantity of RER and SER in a cell can slowly interchange from one type to the other, depending on changing metabolic needs. Transformation can include embedment of new proteins in membrane as well as structural changes. Massive changes may also occur in protein content without noticeable structural changes.
   
===Rough endoplasmic reticulum===
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===Rough endoplasmic ret likes in the bum===
 
[[Image:Translation.gif|thumb|300px|An animation showing how a protein destined for the [[secretory pathway]] is synthesized into the rough endoplasmic reticulum (which appears at upper right in animation when approximately half of its time has passed).]]
 
[[Image:Translation.gif|thumb|300px|An animation showing how a protein destined for the [[secretory pathway]] is synthesized into the rough endoplasmic reticulum (which appears at upper right in animation when approximately half of its time has passed).]]
 
The surface of the rough endoplasmic reticulum (RER) is studded with protein-manufacturing [[ribosome]]s giving it a "rough" appearance (hence its name). The binding site of the Ribosome on RER is the [[translocon]].<ref>{{cite journal | author= Görlich D, Prehn S, Hartmann E, Kalies KU, Rapoport TA. | title= A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation. | journal= Cell | year=1992 |month=Oct.| volume=71 | issue=3 | pages=489-503 | pmid=1423609 }}</ref> However, the ribosomes bound to the RER at any one time are not a stable part of this organelle's structure as ribosomes are constantly being bound and released from the membrane. A ribosome binds to the ER only when it begins to synthesize a protein destined for the [[secretory pathway]].<ref name="lodish">Lodish, Harvey, et al. (2003) ''Molecular Cell Biology 5th Edition''. W. H. Freeman, pp. 659-666 ISBN 0-7167-4366-3</ref> Here, a ribosome in the cytosol begins synthesizing a protein until a [[signal recognition particle]] recognizes the [[signal peptide]] of 5-30 [[hydrophobic]] [[amino acid]]s, sometimes preceded by a positively charged amino acid. This signal sequence allows the recognition particle to bind to the ribosome, causing the ribosome to bind to the RER and pass the new protein through the ER membrane. The signal peptide is then cleaved off within the lumen of the ER. Ribosomes at this point may be released back into the cytosol, however non-translating ribosomes are also known to stay associated with translocons. <ref name="Seiser2000">{{cite journal|last1=Seiser|first1=R. M.|title=The Fate of Membrane-bound Ribosomes Following the Termination of Protein Synthesis|journal=Journal of Biological Chemistry|volume=275|issue=43|year=2000|pages=33820–33827|issn=00219258|doi=10.1074/jbc.M004462200}}</ref>
 
The surface of the rough endoplasmic reticulum (RER) is studded with protein-manufacturing [[ribosome]]s giving it a "rough" appearance (hence its name). The binding site of the Ribosome on RER is the [[translocon]].<ref>{{cite journal | author= Görlich D, Prehn S, Hartmann E, Kalies KU, Rapoport TA. | title= A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation. | journal= Cell | year=1992 |month=Oct.| volume=71 | issue=3 | pages=489-503 | pmid=1423609 }}</ref> However, the ribosomes bound to the RER at any one time are not a stable part of this organelle's structure as ribosomes are constantly being bound and released from the membrane. A ribosome binds to the ER only when it begins to synthesize a protein destined for the [[secretory pathway]].<ref name="lodish">Lodish, Harvey, et al. (2003) ''Molecular Cell Biology 5th Edition''. W. H. Freeman, pp. 659-666 ISBN 0-7167-4366-3</ref> Here, a ribosome in the cytosol begins synthesizing a protein until a [[signal recognition particle]] recognizes the [[signal peptide]] of 5-30 [[hydrophobic]] [[amino acid]]s, sometimes preceded by a positively charged amino acid. This signal sequence allows the recognition particle to bind to the ribosome, causing the ribosome to bind to the RER and pass the new protein through the ER membrane. The signal peptide is then cleaved off within the lumen of the ER. Ribosomes at this point may be released back into the cytosol, however non-translating ribosomes are also known to stay associated with translocons. <ref name="Seiser2000">{{cite journal|last1=Seiser|first1=R. M.|title=The Fate of Membrane-bound Ribosomes Following the Termination of Protein Synthesis|journal=Journal of Biological Chemistry|volume=275|issue=43|year=2000|pages=33820–33827|issn=00219258|doi=10.1074/jbc.M004462200}}</ref>
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