• Corpus ID: 14709886

Functional characterisation of Rab22a and Munc18b, two proteins regulating vesicle transport in mammalian cells

@inproceedings{Kauppi2004FunctionalCO,
  title={Functional characterisation of Rab22a and Munc18b, two proteins regulating vesicle transport in mammalian cells},
  author={Maria Kauppi},
  year={2004}
}
V SUMMARY AND CONCLUSIONS 59 VI ACKNOWLEDGEMENTS 62 VII REFERENCES 63 5 ORIGINAL PUBLICATIONS This thesis is based on the following articles, which are in the text referred to their Roman numerals. In addition, some unpublished results are presented. (2001) The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking. (2000) Munc18-2, a functional partner of syntaxin 3, controls apical membrane trafficking in epithelial cells. (2002) Analysis of the Munc18b-syntaxin… 
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The data suggest a model whereby Cdk5 acts to regulate Munc18a interaction with syntaxin 1a and thereby modulates the level of vesicle SNARE interaction withntaxin 1 a and secretory responsiveness.

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The cloning and molecular characterization of a Sec1-related protein expressed in the MDCK epithelial cell line is reported, identifying Munc-18-2 as a predominantly epithelial vesicle-transport protein with a polarized distribution and provided novel in vivo evidence for the association of Sec 1-related proteins with members of the syntaxin family.

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It is shown that recombinant Munc-18 is phosphorylated by conventional PKC in a Ca- and phospholipid-dependent manner in a cell-free system and this results suggest that the PKC-catalyzed phosphorylation of Munm-18 plays an important role in regulating the interaction of MunC-18 with syntaxin and thereby the docking and/or the fusion of synaptic vesicles with the presynaptic plasma membrane.

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