ArticleThe Journal of general physiology2017
Slow fusion pore expansion creates a unique reaction chamber for co-packaged cargo.
Article in The Journal of general physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- PACAP and acetylcholine cause distinct Ca2+ signals and secretory responses in chromaffin cells.The Journal of general physiology · 2023Article
- High-speed imaging reveals the bimodal nature of dense core vesicle exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- VAMP2 and synaptotagmin mobility in chromaffin granule membranes: implications for regulated exocytosis.Molecular biology of the cell · 2022Article
- Synaptotagmin-7 enhances calcium-sensing of chromaffin cell granules and slows discharge of granule cargos.Journal of neurochemistry · 2020Article
- Fusion Pore Expansion and Contraction during Catecholamine Release from Endocrine Cells.Biophysical journal · 2020Article
- Identification of β-synuclein on secretory granules in chromaffin cells and the effects of α- and β-synuclein on post-fusion BDNF discharge and fusion pore expansion.Neuroscience letters · 2019Article
- Unraveling the mechanisms of calcium-dependent secretion.The Journal of general physiology · 2019Review
- Chromogranin A, the major lumenal protein in chromaffin granules, controls fusion pore expansion.The Journal of general physiology · 2019Article
- The fusion pore, 60 years after the first cartoon.FEBS letters · 2018Review
- The synaptotagmin C2B domain calcium-binding loops modulate the rate of fusion pore expansion.Molecular biology of the cell · 2018Article
- Chemistry in a vesicle.The Journal of general physiology · 2017Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A lumenal secretory granule protein, tissue plasminogen activator (tPA), greatly slows fusion pore dilation and thereby slows its own discharge. We investigated another outcome of the long-lived narrow fusion pore: the creation of a nanoscale chemical reaction chamber for granule contents in which the pH is suddenly neutralized upon fusion. Bovine adrenal chromaffin cells endogenously express both tPA and its primary protein inhibitor, plasminogen activator inhibitor 1 (PAI). We found by immunocytochemistry that tPA and PAI are co-packaged in the same secretory granule. It is known that PAI irreversibly and covalently inactivates tPA at neutral pH. We demonstrate with zymography that the acidic granule lumen protects tPA from inactivation by PAI. Immunocytochemistry, total internal reflection fluorescence (TIRF) microscopy, and polarized TIRF microscopy demonstrated that co-packaged PAI and tPA remain together in granules for many seconds in the nanoscale reaction chamber, more than enough time to inhibit tPA and create a new secreted protein species.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.