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Multicolour imaging of post-Golgi sorting and trafficking in live cells

Keller, Patrick, Toomre, Derek, Díaz, Elena, White, Jamie, Simons, Kai·2001·Nature Cell Biology
DOI 10.1038/35055042
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Abstract

The biogenesis and maintenance of asymmetry is crucial to many cellular functions including absorption and secretion, signalling, development and morphogenesis. Here we have directly visualized the segregation and trafficking of apical (glycosyl phosphatidyl inositol-anchored) and basolateral (vesicular stomatitis virus glycoprotein) cargo in living cells using multicolour imaging of green fluorescent protein variants. Apical and basolateral cargo segregate progressively into large domains in Golgi/trans-Golgi network structures, exclude resident proteins, and exit in separate transport containers. These remain distinct and do not merge with endocytic structures suggesting that lateral segregation in the trans-Golgi network is the primary sorting event. Fusion with the plasma membrane was detected by total internal reflection microscopy and reveals differences between apical and basolateral carriers as well as new 'hot spots' for exocytosis.

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  • A crucial mechanism underlying establishment and maintenance of cellular polarity is differential sorting of proteins to distinct plasma membrane domains along the secretory and endosomal pathways.

    “One crucial mechanism underlying establishment and maintenance of cellular polarity is differential sorting of proteins to distinct plasma membrane domains along the secretory and endosomal pathways (Keller et al., 2001;Kreitzer et al., 2003).”

    From SH3TC2, a protein mutant in Charcot–Marie–Tooth neuropathy, links peripheral nerve myelination to endosomal recycling (2010) · cites this paper as Keller et al., 2001

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Metadata

Authors
Keller, P., Toomre, D., Díaz, E., White, J., & Simons, K.
Venue
Nature Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2001-01-15
Volume
3
Issue
2
Pages
140-149
ISSN
  • 1465-7392
  • 1476-4679
DOI
10.1038/35055042
Cited by
398
References
2
Language
en
Licence
www.springer.com/tdm (tdm)

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