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      Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex

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          Abstract

          Recent results have provided increasing evidence for the existence of an intermediate membrane compartment between the rough endoplasmic reticulum and the Golgi complex which seems to function in protein sorting and the regulation of membrane traffic in the early part of the exocytic pathway. Localization of resident marker proteins has shown that this compartment consists of both peripheral and central elements. The aim of the present review is to combine the data on the pre-Golgi compartment with previous ideas of membrane traffic at the ER-Golgi interface. We propose a model which describes how mobile, endosome-like elements of the pre-Golgi compartment function in the generation of the compositional and functional boundary between the widely distributed ER and the more centrally located Golgi stacks.

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          Brefeldin A: insights into the control of membrane traffic and organelle structure

          (1992)
          Article 0 comments Cited 192 times – based on 0 reviews     Review now
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            Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway.

            Tom A. Schweizer, Cynthia Donaldson, Jeffrey Klausner … (1990)
            Characteristics of brefeldin A (BFA)-induced redistribution of Golgi proteins into the endoplasmic reticulum (ER) and its relationship to an ER retrieval pathway were investigated. Retrograde movement of Golgi proteins into the ER occurred via long, tubulovesicular processes extending out of the Golgi along microtubules. Microtubule-disrupting agents (i.e., nocodazole), energy poisons, and reduced temperatures inhibited this pathway. In BFA-treated cells Golgi proteins appeared to cycle between the ER and an intermediate compartment marked by a 53 kd protein. Addition of nocodazole disrupted this dynamic cycle by preferentially inhibiting retrograde movement, causing Golgi proteins to accumulate in the intermediate compartment. In the absence of BFA, such an ER cycling pathway appeared to be followed normally by the 53 kd protein but not by Golgi proteins, as revealed by temperature shift experiments. We propose that BFA induces the interaction of the Golgi with an intermediate "recycling" compartment that utilizes a microtubule-dependent pathway into the ER.
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              Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic.

              Jennifer Lippincott-Schwartz, Lydia C. Yuan, Christopher Tipper … (1991)
              Addition of brefeldin A (BFA) to most cells results in both the formation of extensive, uncoated membrane tubules through which Golgi components redistribute into the ER and the failure to transport molecules out of this mixed ER/Golgi system. In this study we provide evidence that suggests BFA's effects are not limited to the Golgi apparatus but are reiterated throughout the central vacuolar system. Addition of BFA to cells resulted in the tubulation of the endosomal system, the trans-Golgi network (TGN), and lysosomes. Tubule formation of these organelles was specific to BFA, shared near identical pharmacologic characteristics as Golgi tubules and resulted in targeted membrane fusion. Analogous to the mixing of the Golgi with the ER during BFA treatment, the TGN mixed with the recycling endosomal system. This mixed system remained functional with normal cycling between plasma membrane and endosomes, but traffic between endosomes and lysosomes was impaired.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Semin Cell Biol
                Journal ID (iso-abbrev): Semin. Cell Biol
                Title: Seminars in Cell Biology
                Publisher: Published by Elsevier Ltd.
                ISSN (Print): 1043-4682
                ISSN (Electronic): 1043-4682
                Publication date PMC-release: 7 December 2004
                Publication date (Print): October 1992
                Publication date (Electronic): 7 December 2004
                Volume: 3
                Issue: 5
                Pages: 343-355
                Affiliations
                [a ]From the Ludwig Institute for Cancer Research, Stockholm Branch, Box 60202, S-104 01 Stockholm, Sweden
                [b ]From the Department of Biochemistry, University of Helsinki, Unioninkatu 35, SF-00170, Helsinki, Finland
                Author notes
                [‡]

                Present address: Department of Biochemistry, University of Bergen, Årstadveien 19, N-5009 Bergen, Norway.

                Article
                Publisher ID: 1043-4682(92)90020-V
                DOI: 10.1016/1043-4682(92)90020-V
                PMC ID: 7128811
                PubMed ID: 1457777
                SO-VID: 6a965c24-84ea-4ce8-8d76-eeacd8f9169e
                Copyright statement: Copyright © 1992 Published by Elsevier Ltd.
                License:

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

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                Categories
                Subject: Article

                Keywords: endoplasmic reticulum,golgi complex,pre-golgi compartment,protein transport,membrane traffic
                Data availability:
                Keywords: endoplasmic reticulum, golgi complex, pre-golgi compartment, protein transport, membrane traffic

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