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#redirect[[Endoplasmic reticulum]]
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{{BioPsy}}
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[[Image:Protein 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).]]
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The '''endoplasmic reticulum''' ('''ER''') is an [[organelle]] of [[cell (biology)|cells]] in [[eukaryote|eukaryotic organisms]] that forms an interconnected network of membrane vesicles. According to the structure, the endoplasmic reticulum is classified into two types, '''rough endoplasmic reticulum''' '''(RER)''' and [[smooth endoplasmic reticulum]] '''(SER)'''. These are the sites of ''protein synthesis''. The rough endoplasmic reticulum is predominantly found in ''hepatocytes'' where protein synthesis occurs actively.
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The surface of the rough endoplasmic reticulum (often abbreviated RER) is studded with protein-manufacturing [[ribosome]]s giving it a "rough" appearance (hence its name). The binding site of the ribosome on the rough endoplasmic reticulum 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 it at any one time are not a stable part of this organelle's structure as they are constantly being bound and released from the membrane. A ribosome binds to the endoplasmic reticulum only when it begins to synthesize a protein destined for the [[secretory pathway]].<ref name="lodish">{{cite book |last=Lodish |first=Harvey |last2=et al. |year=2003 |title=Molecular Cell Biology |edition=5th |publisher=W. H. Freeman |pages=659–666 |isbn=0-7167-4366-3 }}</ref> There, 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 rough endoplasmic reticulum and pass the new protein through the rough endoplasmic reticulum membrane. The signal peptide is then cleaved off within the lumen of the ER by a signal [[peptidase]]. 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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The membrane of the rough endoplasmic reticulum forms large double membrane sheets that are located near, and continuous with, the outer layer of the [[nuclear envelope]].<ref name="ShibataVoeltz2006">{{cite journal|last1=Shibata|first1=Yoko|last2=Voeltz|first2=Gia K.|last3=Rapoport|first3=Tom A.|title=Rough Sheets and Smooth Tubules|journal=[[Cell (journal)|Cell]] |volume=126|issue=3|year=2006|pages=435–439|issn=00928674|doi=10.1016/j.cell.2006.07.019}}</ref> Although there is no continuous membrane between the endoplasmic reticulum and the [[Golgi apparatus]], membrane-bound vesicles shuttle proteins between these two compartments.<ref>Endoplasmic reticulum. (n.d.). [[McGraw-Hill Encyclopedia of Science and Technology]]. Retrieved September 13, 2006, from Answers.com Web site: http://www.answers.com/topic/endoplasmic-reticulum</ref> Vesicles are surrounded by coating proteins called COPI and COPII. [[COPII]] targets vesicles to the golgi apparatus and [[COPI]] marks them to be brought back to the rough endoplasmic reticulum. The rough endoplasmic reticulum works in concert with the [[golgi complex]] to [[protein targeting|target new proteins]] to their proper destinations. A second method of transport out of the endoplasmic reticulum involves areas called [[membrane contact site]]s, where the membranes of the endoplasmic reticulum and other organelles are held closely together, allowing the transfer of lipids and other small molecules.<ref>{{cite journal |author=Levine T |title=Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions |journal=Trends Cell Biol. |volume=14 |issue=9 |pages=483–90 |year=2004 |month=September |pmid=15350976 |doi=10.1016/j.tcb.2004.07.017 |url= }}</ref><ref>{{cite journal |author=Levine T, Loewen C |title=Inter-organelle membrane contact sites: through a glass, darkly |journal=Curr. Opin. Cell Biol. |volume=18 |issue=4 |pages=371–8 |year=2006 |month=August |pmid=16806880 |doi=10.1016/j.ceb.2006.06.011}}</ref>
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The rough endoplasmic reticulum is key in multiple functions:
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*Manufacture of [[Lysosome|lysosomal]] enzymes with a [[mannose-6-phosphate]] marker added in the ''cis''-Golgi network{{citation needed|date=December 2012}}
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*Manufacture of [[Secretion|secreted]] proteins, either secreted constitutively with no tag or secreted in a regulatory manner involving [[clathrin]] and paired basic amino acids in the [[signal peptide]].
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*[[Integral membrane proteins]] that stay embedded in the membrane as vesicles exit and bind to new membranes. [[Rab (G-protein)|Rab]] proteins are key in targeting the membrane; [[SNAP-25|SNAP]] and [[SNARE]] proteins are key in the fusion event.
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*Initial [[glycosylation]] as assembly continues. This is N-linked (O-linking occurs in the golgi).
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**N-linked glycosylation: If the protein is properly folded, [[glycosyltransferase]] recognizes the AA sequence [[Asparagine|N]]X[[serine|S]] or [[Asparagine|N]]X[[threonine|T]] (with the S/T residue phosphorylated) and adds a 14-sugar backbone (2-''N''-acetylglucosamine, 9-branching [[mannose]], and 3-[[glucose]] at the end) to the side-chain [[nitrogen]] of Asn.
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==See also==
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==References==
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<references/>
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==Further reading==
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[[Category:Organelles]]
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{{enWP|Endoplasmic reticulum}}

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File:Protein translation.gif

The endoplasmic reticulum (ER) is an organelle of cells in eukaryotic organisms that forms an interconnected network of membrane vesicles. According to the structure, the endoplasmic reticulum is classified into two types, rough endoplasmic reticulum (RER) and smooth endoplasmic reticulum (SER). These are the sites of protein synthesis. The rough endoplasmic reticulum is predominantly found in hepatocytes where protein synthesis occurs actively.

The surface of the rough endoplasmic reticulum (often abbreviated RER) is studded with protein-manufacturing ribosomes giving it a "rough" appearance (hence its name). The binding site of the ribosome on the rough endoplasmic reticulum is the translocon.[1] However, the ribosomes bound to it at any one time are not a stable part of this organelle's structure as they are constantly being bound and released from the membrane. A ribosome binds to the endoplasmic reticulum only when it begins to synthesize a protein destined for the secretory pathway.[2] There, a ribosome in the cytosol begins synthesizing a protein until a signal recognition particle recognizes the signal peptide of 5–30 hydrophobic amino acids, 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 rough endoplasmic reticulum and pass the new protein through the rough endoplasmic reticulum membrane. The signal peptide is then cleaved off within the lumen of the ER by a signal peptidase. Ribosomes at this point may be released back into the cytosol; however, non-translating ribosomes are also known to stay associated with translocons.[3]

The membrane of the rough endoplasmic reticulum forms large double membrane sheets that are located near, and continuous with, the outer layer of the nuclear envelope.[4] Although there is no continuous membrane between the endoplasmic reticulum and the Golgi apparatus, membrane-bound vesicles shuttle proteins between these two compartments.[5] Vesicles are surrounded by coating proteins called COPI and COPII. COPII targets vesicles to the golgi apparatus and COPI marks them to be brought back to the rough endoplasmic reticulum. The rough endoplasmic reticulum works in concert with the golgi complex to target new proteins to their proper destinations. A second method of transport out of the endoplasmic reticulum involves areas called membrane contact sites, where the membranes of the endoplasmic reticulum and other organelles are held closely together, allowing the transfer of lipids and other small molecules.[6][7]

The rough endoplasmic reticulum is key in multiple functions:

  • Manufacture of lysosomal enzymes with a mannose-6-phosphate marker added in the cis-Golgi network[citation needed]
  • Manufacture of secreted proteins, either secreted constitutively with no tag or secreted in a regulatory manner involving clathrin and paired basic amino acids in the signal peptide.
  • Integral membrane proteins that stay embedded in the membrane as vesicles exit and bind to new membranes. Rab proteins are key in targeting the membrane; SNAP and SNARE proteins are key in the fusion event.
  • Initial glycosylation as assembly continues. This is N-linked (O-linking occurs in the golgi).
    • N-linked glycosylation: If the protein is properly folded, glycosyltransferase recognizes the AA sequence NXS or NXT (with the S/T residue phosphorylated) and adds a 14-sugar backbone (2-N-acetylglucosamine, 9-branching mannose, and 3-glucose at the end) to the side-chain nitrogen of Asn.

See alsoEdit

ReferencesEdit

  1. Görlich D, Prehn S, Hartmann E, Kalies KU, Rapoport TA. (Oct. 1992). A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation.. Cell 71 (3): 489–503.
  2. Lodish, Harvey (2003). Molecular Cell Biology, 5th, 659–666, W. H. Freeman.
  3. (2000). The Fate of Membrane-bound Ribosomes Following the Termination of Protein Synthesis. Journal of Biological Chemistry 275 (43): 33820–33827.
  4. (2006). Rough Sheets and Smooth Tubules. Cell 126 (3): 435–439.
  5. Endoplasmic reticulum. (n.d.). McGraw-Hill Encyclopedia of Science and Technology. Retrieved September 13, 2006, from Answers.com Web site: http://www.answers.com/topic/endoplasmic-reticulum
  6. Levine T (September 2004). Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol. 14 (9): 483–90.
  7. Levine T, Loewen C (August 2006). Inter-organelle membrane contact sites: through a glass, darkly. Curr. Opin. Cell Biol. 18 (4): 371–8.

Further readingEdit

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