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Volumn 10, Issue 4, 1998, Pages 542-549

The role of ankyrin and spectrin in membrane transport and domain formation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ANKYRIN; PHOSPHATIDYLINOSITIDE; SPECTRIN;

EID: 0032145247     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80071-9     Document Type: Article
Times cited : (119)

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    • of outstanding interest. The authors give a comparison of amino-peptidase I targeting in rich media and starvation conditions, demonstrating that structures morphologically similar to autophagosomes form in rich media and are used for the specific targeting of amino-peptidase I. The vesicles formed in rich media are called Cvt vesicles and are smaller than autophagosomes and do not appear to include bulk cytosol.
    • Baba M, Osumi M, Scott SV, Klionsky DJ, Ohsumi Y. Two distinct pathways for targeting proteins from the cytoplasm to the vacuole/lysosome. of outstanding interest J Cell Biol. 139:1997;1687-1695 The authors give a comparison of amino-peptidase I targeting in rich media and starvation conditions, demonstrating that structures morphologically similar to autophagosomes form in rich media and are used for the specific targeting of amino-peptidase I. The vesicles formed in rich media are called Cvt vesicles and are smaller than autophagosomes and do not appear to include bulk cytosol.
    • (1997) J Cell Biol , vol.139 , pp. 1687-1695
    • Baba, M.1    Osumi, M.2    Scott, S.V.3    Klionsky, D.J.4    Ohsumi, Y.5
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    • 0030807624 scopus 로고    scopus 로고
    • A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole
    • of special interest. This paper describes the characterization of the vacuolar t-SNARE Vam3p. Vam3p is necessary for the correct targeting of multiple vacuolar hydrolases. In addition, both autophagy and cytoplasm-to-vacuole transport are disrupted in temperature-sensitive vam3 cells, suggesting that Vam3p is a multispecificity receptor for fusion at the vacuole membrane.
    • Darsow T, Rieder SE, Emr SD. A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. of special interest J Cell Biol. 138:1997;517-529 This paper describes the characterization of the vacuolar t-SNARE Vam3p. Vam3p is necessary for the correct targeting of multiple vacuolar hydrolases. In addition, both autophagy and cytoplasm-to-vacuole transport are disrupted in temperature-sensitive vam3 cells, suggesting that Vam3p is a multispecificity receptor for fusion at the vacuole membrane.
    • (1997) J Cell Biol , vol.138 , pp. 517-529
    • Darsow, T.1    Rieder, S.E.2    Emr, S.D.3
  • 52
    • 0030940407 scopus 로고    scopus 로고
    • Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in the yeast Saccharomyces cerevisiae
    • Nakamura N, Hirata A, Ohsumi Y, Wada Y. Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in the yeast Saccharomyces cerevisiae. J Biol Chem. 272:1997;11344-11349.
    • (1997) J Biol Chem , vol.272 , pp. 11344-11349
    • Nakamura, N.1    Hirata, A.2    Ohsumi, Y.3    Wada, Y.4
  • 53
    • 0030830765 scopus 로고    scopus 로고
    • A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole
    • of special interest. This paper demonstrates that Vps18p function is required for biosynthetic, endocytic and autophagic protein transport to the vacuole.
    • Rieder SE, Emr SD. A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole. of special interest Mol Biol Cell. 8:1997;2307-2327 This paper demonstrates that Vps18p function is required for biosynthetic, endocytic and autophagic protein transport to the vacuole.
    • (1997) Mol Biol Cell , vol.8 , pp. 2307-2327
    • Rieder, S.E.1    Emr, S.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.