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Sortilin Is the Major 110-kDa Protein in GLUT4 Vesicles from Adipocytes

Morris, Nicholas J., Ross, Stuart A., Lane, William S., Moestrup, Søren K., Petersen, Claus M., Keller, Susanna R., Lienhard, Gustav E.·1998·Journal of Biological Chemistry
DOI 10.1074/jbc.273.6.3582
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  • Previous evidence on sortilin and MPR300 co-localization supports full-length sortilin as a functional sorting receptor.

    “This is in good agreement with previous evidence on sortilin and MPR300 co-localization, and in strong support of full-length sortilin as a functional sorting receptor (Petersen et al., 1997;Morris et al., 1998).”

    From The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein (2001) · cites this paper as Morris et al., 1998

    The Abstract (page unavailable) reports that sortilin appears to colocalize with CIM6PR (MPR300) in COS cells and says this suggests a sorting-receptor role. The Discussion (page unavailable) says sortilin’s function remains undetermined and that it could instead be a receptor for an extracellular ligand. The source therefore supports the prior colocalization and the proposed role, but not an established function for full-length sortilin as a sorting receptor. (LLM, conf=0.86)

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  • Sortilin predominates in intracellular compartments, with only a minor fraction on the cell surface and about 90% in Golgi and vesicles co-localizing with MPR300.

    “Only a minor fraction of the receptors is expressed on the cell surface, whereas ~90% are found in Golgi and vesicles, showing extensive co-localization with MPR300 (Petersen et al., 1997;Morris et al., 1998).”

    From The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein (2001) · cites this paper as Morris et al., 1998

    The Abstract says sortilin is largely located in intracellular GLUT4-containing vesicles in adipocytes and reports apparent co-localization with the cation-independent mannose 6-phosphate receptor in COS cells. The results on vesicle isolation report 70–75% of sortilin in the sampled fraction in GLUT4 vesicles, not that ~90% of all sortilin is in Golgi and vesicles; the paper also does not quantify the fraction at the cell surface. Pages are not specified in our copy. (LLM, conf=0.87)

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Metadata

Authors
Morris, N. J., Ross, S. A., Lane, W. S., Moestrup, S. K., Petersen, C. M., Keller, S. R., & Lienhard, G. E.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-02
Volume
273
Issue
6
Pages
3582-3587
ISSN
0021-9258
DOI
10.1074/jbc.273.6.3582
Cited by
130
References
0
Language
en
Licence

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