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Alterations in the protein composition of maturing phagosomes.
- A. Pitt, L. Mayorga, P. Stahl, A. Schwartz
- BiologyThe Journal of clinical investigation
- 1 November 1992
Although the macrophage phagosome's total protein composition changes little during phagolysosome formation, the maturing phagosomes both receives and eliminates proteins, possibly by protein recycling, specific membrane and sequestered proteins.
On the killing of mycobacteria by macrophages
EM analysis showed clearly that all the mycobacteria remained within phagosomes even at late times of infection, and theoretical modelling of the data identified two different potential sets of explanations that are consistent with the results.
Rab22a Regulates the Sorting of Transferrin to Recycling Endosomes
- Javier G. Magadán, M. Barbieri, R. Mesa, P. Stahl, L. Mayorga
- BiologyMolecular and Cellular Biology
- 1 April 2006
It is speculated that Rab22a controls the transport of the transferrin receptor from sorting to recycling endosomes and depletion by small interfering RNA disorganized the perinuclear recycling center and strongly inhibited transferrin recycling.
Acrosomal exocytosis, a special type of regulated secretion
The acrosome is a single secretory granule present in the head of mammalian ‐ and other animal groups ‐ sperm and because of its particular characteristics, acrosomal exocytosis is a unique mammalian model for the study of the different steps of the membrane fusion cascade.
Calcium-induced Acrosomal Exocytosis Requires cAMP Acting through a Protein Kinase A-independent, Epac-mediated Pathway*
CAMP-elicited exocytosis was sensitive to anti-α-SNAP, anti-NSF, and anti-Rab3A antibodies, to intra-acrosomal Ca2+ chelators, and to botulinum toxins but was resistant to cAMP-dependent protein kinase blockers.
Dynamics of SNARE Assembly and Disassembly during Sperm Acrosomal Exocytosis
It is shown that, in unactivated sperm, SNAREs are locked in heterotrimeric cis complexes, and the unidirectional and sequential disassembly and assembly of SNARE complexes drive acrosomal exocytosis.
Membrane trafficking along the phagocytic pathway.
Transport of phagosomal components to an endosomal compartment.
PTP1B Dephosphorylates N-Ethylmaleimide-sensitive Factor and Elicits SNARE Complex Disassembly during Human Sperm Exocytosis*
- Valeria E P Zarelli, M. C. Ruete, C. Roggero, L. Mayorga, C. Tomes
- Biology, ChemistryJournal of Biological Chemistry
- 17 April 2009
It is demonstrated that phosphorylation of NSF on tyrosine residues prevents its SNARE complex dissociation activity and establish for the first time a role for PTP1B in the modulation of the membrane fusion machinery.
Vesicle fusion following receptor-mediated endocytosis requires a protein active in Golgi transport
It is shown that the same N-ethylmaleimide-sensitive factor that catalyses the vesicle-mediated transport within Golgi stacks is also required for endocytic vesicles fusion, suggesting that a common mechanism for vESicle fusion exists for both the secretory and endocytical pathways of eukaryotic cells.