ArticleMolecular biology of the cell2000
Sorting to synaptic-like microvesicles from early and late endosomes requires overlapping but not identical targeting signals.
Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Trafficking of vesicular neurotransmitter transporters.Traffic (Copenhagen, Denmark) · 2008Review
- Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin.Molecular biology of the cell · 2004Article
- Ligand-induced internalization of the p75 neurotrophin receptor: a slow route to the signaling endosome.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Selective and signal-dependent recruitment of membrane proteins to secretory granules formed by heterologously expressed von Willebrand factor.Molecular biology of the cell · 2002Article
- Rab4 regulates formation of synaptic-like microvesicles from early endosomes in PC12 cells.Molecular biology of the cell · 2001Article
- A conserved mechanism of synaptogyrin localization.Molecular biology of the cell · 2001Article
- AP-3 mediates tyrosinase but not TRP-1 trafficking in human melanocytes.Molecular biology of the cell · 2001Article
- Cyclic AMP increases cell surface expression of functional Na,K-ATPase units in mammalian cortical collecting duct principal cells.Molecular biology of the cell · 2001Article
- Rapid transport of internalized P-selectin to late endosomes and the TGN: roles in regulating cell surface expression and recycling to secretory granules.The Journal of cell biology · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In PC12 neuroendocrine cells, synaptic-like microvesicles (SLMV) are thought to be formed by two pathways. One pathway sorts the proteins to SLMV directly from the plasma membrane (or a specialized domain thereof) in an adaptor protein complex 2-dependent, brefeldin A (BFA)-insensitive manner. Another pathway operates via an endosomal intermediate, involves adaptor protein complex 3, and is BFA sensitive. We have previously shown that when expressed in PC12 cells, HRP-P-selectin chimeras are directed to SLMV mostly via the endosomal, BFA-sensitive route. We have now found that two endosomal intermediates are involved in targeting of HRP-P-selectin chimeras to SLMV. The first intermediate is the early, transferrin-positive, epidermal growth factor-positive endosome, from which exit to SLMV is controlled by the targeting determinants YGVF and KCPL, located within the cytoplasmic domain of P-selectin. The second intermediate is the late, transferrin-negative, epidermal growth factor-positive late endosome, from where HRP-P-selectin chimeras are sorted to SLMV in a YGVF- and DPSP-dependent manner. Both sorting steps, early endosomes to SLMV and late endosomes to SLMV, are affected by BFA. In addition, analysis of double mutants with alanine substitutions of KCPL and YGVF or KCPL and DPSP indicated that chimeras pass sequentially through these intermediates en route both to lysosomes and to SLMV. We conclude that a third site of formation for SLMV, the late endosomes, exists in PC12 cells.
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