O-glycosylation is essential for intracellular targeting of synaptotagmins I and II in non-neuronal specialized secretory cells
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Atiya-Nasagi, Y
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机构:Tel Aviv Univ, Sackler Sch Med, Dept Cell & Dev Biol, IL-69978 Tel Aviv, Israel
Atiya-Nasagi, Y
Cohen, H
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机构:Tel Aviv Univ, Sackler Sch Med, Dept Cell & Dev Biol, IL-69978 Tel Aviv, Israel
Cohen, H
Medalia, O
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机构:Tel Aviv Univ, Sackler Sch Med, Dept Cell & Dev Biol, IL-69978 Tel Aviv, Israel
Medalia, O
Fukuda, M
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机构:Tel Aviv Univ, Sackler Sch Med, Dept Cell & Dev Biol, IL-69978 Tel Aviv, Israel
Fukuda, M
Sagi-Eisenberg, R
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Tel Aviv Univ, Sackler Sch Med, Dept Cell & Dev Biol, IL-69978 Tel Aviv, IsraelTel Aviv Univ, Sackler Sch Med, Dept Cell & Dev Biol, IL-69978 Tel Aviv, Israel
Sagi-Eisenberg, R
[1
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[1] Tel Aviv Univ, Sackler Sch Med, Dept Cell & Dev Biol, IL-69978 Tel Aviv, Israel
[2] RIKEN, Fukuda Initiat Res Unit, Wako, Saitama 3510198, Japan
We have examined the trafficking of synaptotagmin (Syt) I and II in the mast cell line rat basophilic leukemia (RBL2H3). We demonstrate that both Syt I and Syt II travel through the plasma membrane and require endocytosis to reach their final intracellular localization. However, N- or C-terminal tagging of Syt II, but not of Syt I, prevents its internalization, trapping the tagged protein at the plasma membrane. Furthermore, a chimeric protein comprising a tagged luminal domain of Syt II fused with the remaining domains of Syt I also localizes to the plasma membrane, whereas a chimera consisting of tagged luminal domain of Syt I fused with Syt II colocalizes with Syt I on secretory granules. We also show that endocytosis of both Syt I and Syt II is strictly dependent on O-glycosylation processing, whereby O-glycosylation mutants of either protein fail to internalize and remain at the plasma membrane. Our results indicate that the luminal domains of Syt I and Syt II govern their internalization capacity from the plasma membrane and identify O-glycosylation as playing a crucial role in Syt trafficking in non-neuronal secretory cells.
机构:Tel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, Israel
Barzilay, E
Ben-Califa, N
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机构:Tel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, Israel
Ben-Califa, N
Supino-Rosin, L
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机构:Tel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, Israel
Supino-Rosin, L
Kashman, Y
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机构:Tel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, Israel
Kashman, Y
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Hirschberg, K
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Elazar, Z
Neumann, D
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Tel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, IsraelTel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, Israel
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Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USAUniv Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA
Dasgupta, S
Kelly, RB
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Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USAUniv Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA
机构:Tel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, Israel
Barzilay, E
Ben-Califa, N
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机构:Tel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, Israel
Ben-Califa, N
Supino-Rosin, L
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机构:Tel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, Israel
Supino-Rosin, L
Kashman, Y
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机构:Tel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, Israel
Kashman, Y
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Hirschberg, K
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Elazar, Z
Neumann, D
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Tel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, IsraelTel Aviv Univ, Sackler Fac Med, Dept Cell & Dev Biol, IL-69978 Ramat Aviv, Israel
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Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USAUniv Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA
Dasgupta, S
Kelly, RB
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Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USAUniv Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA