Endoplasmic Reticulum funtion?

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    • #4791
      student12
      Participant

      After the ribosomes synthesise polypeptides they pass into the lumen of the ER where they can be added sugar molecules to make glycoproteins.

      Question: Is this also where polypeptides are modified for example being cleaved by protease to form functional proteins?
      Also where chaperone proteins help the protein fold correctly into its tertiary structure?

    • #48392
      rg
      Participant

      the final processing to protiens(like gycosylation etc.) is done in golgi complex….ER transports synthesised substances…but they may also participate in works like detoxification in liver by smooth ER…..chaperones do this possibly in the cytoplasm….

    • #48403
      LilKim
      Participant

      chaperones are present in the ER… and initially they help keep protiens unfolded… and eventually they help fold the proteins at the appropriate time (at a certain point during translation… or after translation)

      However, many proteins are folded before the get to the golgi.

    • #55924
      jacob mack
      Participant
      quote LilKim:

      chaperones are present in the ER… and initially they help keep protiens unfolded… and eventually they help fold the proteins at the appropriate time (at a certain point during translation… or after translation)

      However, many proteins are folded before the get to the golgi.

      That is true, ER helps transport necessary products to the cell membrane as it is connected to it; (e.g. glycoproteins ect…) and so chaperones would be necessary in some cases of pre– ER transport to facilitate modification for immeduate use.

    • #55938
      sporkius
      Participant

      http://www.projectuniv.org/Biology/GeneralBiology1.htm

      I wrote this a couple weeks ago. You might want to look at it. It covers everything in this post and more. Hope it will help.

    • #55980
      MrMistery
      Participant

      a little too basic and contains some wrong info.

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