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Volumn 15, Issue 4, 2003, Pages 438-445

Retrograde traffic in the biosynthetic-secretory route: Pathways and machinery

Author keywords

[No Author keywords available]

Indexed keywords

LIPID; MEMBRANE PROTEIN;

EID: 0043268861     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(03)00077-2     Document Type: Review
Times cited : (75)

References (55)
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    • •] represent two of several recent studies on this novel tethering complex (reviewed in [55]), which share homology to the yeast exocyst and the trans-Golgi-network-associated GARP complex.
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    • Retrograde transport of protein toxins under conditions of COPI dysfunction
    • The authors studied the role of the COPI machinery in retrograde transport of protein toxins using mutant Chinese hamster ovary (ldlF) cells with a temperature-sensitive defect in the ε-COP subunit of COPI coats, and cyclohexane-bismethylamine, a compound that blocks COPI binding to membranes. Unexpectedly, they find that cells under these conditions remain sensitive to toxins, irrespective of whether or not they contain a KDEL (or KDEL-like) sequence. These data support the existence of a COPI-independent pathway from the trans-Golgi network to the ER, and suggest that the mechanisms of the COPI-dependent and -independent pathways are closely linked
    • Chen A., Mikoryak C., Draper R.K. Retrograde transport of protein toxins under conditions of COPI dysfunction. Biochim. Biophys. Acta. 1589:2002;124-139 The authors studied the role of the COPI machinery in retrograde transport of protein toxins using mutant Chinese hamster ovary (ldlF) cells with a temperature-sensitive defect in the ε-COP subunit of COPI coats, and cyclohexane-bismethylamine, a compound that blocks COPI binding to membranes. Unexpectedly, they find that cells under these conditions remain sensitive to toxins, irrespective of whether or not they contain a KDEL (or KDEL-like) sequence. These data support the existence of a COPI-independent pathway from the trans-Golgi network to the ER, and suggest that the mechanisms of the COPI-dependent and -independent pathways are closely linked.
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    • This paper shows that Rab6 directly interacts with Bicaudal-D1 (BICD1), one of the two mammalian homologues of Drosophila Bicaudal-D. Rab6 may serve as a receptor for BICD1, which then recruits the dynein-dynactin complex on Golgi and/or Golgi-derived membranes. This study provides a molecular basis for the bidirectional movement along microtubules of Golgi-to-ER transport intermediates defined by Rab6A (COPI-independent transport)
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    • Structure of the Golgi and distribution of reporter molecules at 20°C reveals the complexity of the exit compartments
    • Rapid freezing techniques, high-resolution electron microscope tomography, and three-dimensional reconstruction of serial sections were applied to investigate Golgi structure in NRK cells incubated at 20°C, which blocks protein exit from the Golgi complex. The disappearance of trans-Golgi tubules was accompanied by lateral bulging of the three trans-most cisternae, suggesting that exit occurs from multiple trans-cisternae. In this study, the authors also characterise further a specialised ER domain that intimately associates with several trans-cisternae, suggesting a direct route for exchange of material between trans-Golgi and the ER
    • Ladinsky M.S., Wu C.C., McIntosh S., McIntosh J.R., Howell K.E. Structure of the Golgi and distribution of reporter molecules at 20°C reveals the complexity of the exit compartments. Mol. Biol. Cell. 13:2002;2810-2825 Rapid freezing techniques, high-resolution electron microscope tomography, and three-dimensional reconstruction of serial sections were applied to investigate Golgi structure in NRK cells incubated at 20°C, which blocks protein exit from the Golgi complex. The disappearance of trans-Golgi tubules was accompanied by lateral bulging of the three trans-most cisternae, suggesting that exit occurs from multiple trans-cisternae. In this study, the authors also characterise further a specialised ER domain that intimately associates with several trans-cisternae, suggesting a direct route for exchange of material between trans-Golgi and the ER.
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    • Cytoplasmic linker proteins (CLIPs) are non-motor microtubule-binding proteins. The authors have characterised a novel CLIP protein, CLIPR-59, that is localised to trans-Golgi network (TGN) membranes. CLIP-59 could be involved in early/recycling endosome-TGN dynamics
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.