Gi Protein Modulation of the Potassium Channel TASK-2 Mediates Vesicle Osmotic Swelling to Facilitate the Fusion of Aquaporin-2 Water Channel Containing Vesicles. Centrone, M., De Santo, M. P., Nicotera, I., Labate, C., Ranieri, M., Di Mise, A., Mola, M. G., Mastrodonato, M., Elliani, R., Barberi, R., Formoso, V., Tamma, G., & Valenti, G. CELLS, DEC, 2018. doi abstract bibtex Vesicle fusion is a fundamental cell biological process similar from yeasts to humans. For secretory vesicles, swelling is considered a step required for the expulsion of intravesicular content. Here this concept is revisited providing evidence that it may instead represent a general mechanism. We report the first example that non-secretory vesicles, committed to insert the Aquaporin-2 water channel into the plasma membrane, swell and this phenomenon is required for fusion to plasma membrane. Through an interdisciplinary approach, using atomic force microscope (AFM), a fluorescence-based assay of vesicle volume changes and NMR spectroscopy to measure water self-diffusion coefficient, we provide evidence that Gi protein modulation of potassium channel TASK-2 localized in AQP2 vesicles, is required for vesicle swelling. Estimated intravesicular K+ concentration in AQP2 vesicles, as measured by inductively coupled plasma mass spectrometry, was 5.3 mM, demonstrating the existence of an inwardly K+ chemical gradient likely generating an osmotic gradient causing vesicle swelling upon TASK-2 gating. Of note, abrogation of K+ gradient significantly impaired fusion between vesicles and plasma membrane. We conclude that vesicle swelling is a potentially important prerequisite for vesicle fusion to the plasma membrane and may be required also for other non-secretory vesicles, depicting a general mechanism for vesicle fusion.
@article{ ISI:000455320700054,
Author = {Centrone, Mariangela and De Santo, Maria Penelope and Nicotera, Isabella
and Labate, Cristina and Ranieri, Marianna and Di Mise, Annarita and
Mola, Maria Grazia and Mastrodonato, Maria and Elliani, Rosangela and
Barberi, Riccardo and Formoso, Vincenzo and Tamma, Grazia and Valenti,
Giovanna},
Title = {{Gi Protein Modulation of the Potassium Channel TASK-2 Mediates Vesicle
Osmotic Swelling to Facilitate the Fusion of Aquaporin-2 Water Channel
Containing Vesicles}},
Journal = {{CELLS}},
Year = {{2018}},
Volume = {{7}},
Number = {{12}},
Month = {{DEC}},
Abstract = {{Vesicle fusion is a fundamental cell biological process similar from
yeasts to humans. For secretory vesicles, swelling is considered a step
required for the expulsion of intravesicular content. Here this concept
is revisited providing evidence that it may instead represent a general
mechanism. We report the first example that non-secretory vesicles,
committed to insert the Aquaporin-2 water channel into the plasma
membrane, swell and this phenomenon is required for fusion to plasma
membrane. Through an interdisciplinary approach, using atomic force
microscope (AFM), a fluorescence-based assay of vesicle volume changes
and NMR spectroscopy to measure water self-diffusion coefficient, we
provide evidence that Gi protein modulation of potassium channel TASK-2
localized in AQP2 vesicles, is required for vesicle swelling. Estimated
intravesicular K+ concentration in AQP2 vesicles, as measured by
inductively coupled plasma mass spectrometry, was 5.3 mM, demonstrating
the existence of an inwardly K+ chemical gradient likely generating an
osmotic gradient causing vesicle swelling upon TASK-2 gating. Of note,
abrogation of K+ gradient significantly impaired fusion between vesicles
and plasma membrane. We conclude that vesicle swelling is a potentially
important prerequisite for vesicle fusion to the plasma membrane and may
be required also for other non-secretory vesicles, depicting a general
mechanism for vesicle fusion.}},
DOI = {{10.3390/cells7120276}},
Article-Number = {{276}},
EISSN = {{2073-4409}},
ResearcherID-Numbers = {{Mola, Maria Grazia/I-3507-2019
BARBERI, Riccardo Cristoforo/D-9219-2012
Mastrodonato, Maria/P-4513-2016
}},
ORCID-Numbers = {{Mola, Maria Grazia/0000-0002-4421-9237
NICOTERA, Isabella/0000-0002-4411-0573
BARBERI, Riccardo Cristoforo/0000-0001-9713-1696
Mastrodonato, Maria/0000-0002-0799-8032
FORMOSO, Vincenzo/0000-0003-4887-4893}},
Unique-ID = {{ISI:000455320700054}},
}
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G.","Mastrodonato, M.","Elliani, R.","Barberi, R.","Formoso, V.","Tamma, G.","Valenti, G."],"bibdata":{"bibtype":"article","type":"article","author":[{"propositions":[],"lastnames":["Centrone"],"firstnames":["Mariangela"],"suffixes":[]},{"propositions":[],"lastnames":["De","Santo"],"firstnames":["Maria","Penelope"],"suffixes":[]},{"propositions":[],"lastnames":["Nicotera"],"firstnames":["Isabella"],"suffixes":[]},{"propositions":[],"lastnames":["Labate"],"firstnames":["Cristina"],"suffixes":[]},{"propositions":[],"lastnames":["Ranieri"],"firstnames":["Marianna"],"suffixes":[]},{"propositions":[],"lastnames":["Di","Mise"],"firstnames":["Annarita"],"suffixes":[]},{"propositions":[],"lastnames":["Mola"],"firstnames":["Maria","Grazia"],"suffixes":[]},{"propositions":[],"lastnames":["Mastrodonato"],"firstnames":["Maria"],"suffixes":[]},{"propositions":[],"lastnames":["Elliani"],"firstnames":["Rosangela"],"suffixes":[]},{"propositions":[],"lastnames":["Barberi"],"firstnames":["Riccardo"],"suffixes":[]},{"propositions":[],"lastnames":["Formoso"],"firstnames":["Vincenzo"],"suffixes":[]},{"propositions":[],"lastnames":["Tamma"],"firstnames":["Grazia"],"suffixes":[]},{"propositions":[],"lastnames":["Valenti"],"firstnames":["Giovanna"],"suffixes":[]}],"title":"Gi Protein Modulation of the Potassium Channel TASK-2 Mediates Vesicle Osmotic Swelling to Facilitate the Fusion of Aquaporin-2 Water Channel Containing Vesicles","journal":"CELLS","year":"2018","volume":"7","number":"12","month":"DEC","abstract":"Vesicle fusion is a fundamental cell biological process similar from yeasts to humans. For secretory vesicles, swelling is considered a step required for the expulsion of intravesicular content. Here this concept is revisited providing evidence that it may instead represent a general mechanism. We report the first example that non-secretory vesicles, committed to insert the Aquaporin-2 water channel into the plasma membrane, swell and this phenomenon is required for fusion to plasma membrane. Through an interdisciplinary approach, using atomic force microscope (AFM), a fluorescence-based assay of vesicle volume changes and NMR spectroscopy to measure water self-diffusion coefficient, we provide evidence that Gi protein modulation of potassium channel TASK-2 localized in AQP2 vesicles, is required for vesicle swelling. Estimated intravesicular K+ concentration in AQP2 vesicles, as measured by inductively coupled plasma mass spectrometry, was 5.3 mM, demonstrating the existence of an inwardly K+ chemical gradient likely generating an osmotic gradient causing vesicle swelling upon TASK-2 gating. Of note, abrogation of K+ gradient significantly impaired fusion between vesicles and plasma membrane. We conclude that vesicle swelling is a potentially important prerequisite for vesicle fusion to the plasma membrane and may be required also for other non-secretory vesicles, depicting a general mechanism for vesicle fusion.","doi":"10.3390/cells7120276","article-number":"276","eissn":"2073-4409","researcherid-numbers":"Mola, Maria Grazia/I-3507-2019 BARBERI, Riccardo Cristoforo/D-9219-2012 Mastrodonato, Maria/P-4513-2016 ","orcid-numbers":"Mola, Maria Grazia/0000-0002-4421-9237 NICOTERA, Isabella/0000-0002-4411-0573 BARBERI, Riccardo Cristoforo/0000-0001-9713-1696 Mastrodonato, Maria/0000-0002-0799-8032 FORMOSO, Vincenzo/0000-0003-4887-4893","unique-id":"ISI:000455320700054","bibtex":"@article{ ISI:000455320700054,\nAuthor = {Centrone, Mariangela and De Santo, Maria Penelope and Nicotera, Isabella\n and Labate, Cristina and Ranieri, Marianna and Di Mise, Annarita and\n Mola, Maria Grazia and Mastrodonato, Maria and Elliani, Rosangela and\n Barberi, Riccardo and Formoso, Vincenzo and Tamma, Grazia and Valenti,\n Giovanna},\nTitle = {{Gi Protein Modulation of the Potassium Channel TASK-2 Mediates Vesicle\n Osmotic Swelling to Facilitate the Fusion of Aquaporin-2 Water Channel\n Containing Vesicles}},\nJournal = {{CELLS}},\nYear = {{2018}},\nVolume = {{7}},\nNumber = {{12}},\nMonth = {{DEC}},\nAbstract = {{Vesicle fusion is a fundamental cell biological process similar from\n yeasts to humans. For secretory vesicles, swelling is considered a step\n required for the expulsion of intravesicular content. Here this concept\n is revisited providing evidence that it may instead represent a general\n mechanism. We report the first example that non-secretory vesicles,\n committed to insert the Aquaporin-2 water channel into the plasma\n membrane, swell and this phenomenon is required for fusion to plasma\n membrane. Through an interdisciplinary approach, using atomic force\n microscope (AFM), a fluorescence-based assay of vesicle volume changes\n and NMR spectroscopy to measure water self-diffusion coefficient, we\n provide evidence that Gi protein modulation of potassium channel TASK-2\n localized in AQP2 vesicles, is required for vesicle swelling. Estimated\n intravesicular K+ concentration in AQP2 vesicles, as measured by\n inductively coupled plasma mass spectrometry, was 5.3 mM, demonstrating\n the existence of an inwardly K+ chemical gradient likely generating an\n osmotic gradient causing vesicle swelling upon TASK-2 gating. Of note,\n abrogation of K+ gradient significantly impaired fusion between vesicles\n and plasma membrane. We conclude that vesicle swelling is a potentially\n important prerequisite for vesicle fusion to the plasma membrane and may\n be required also for other non-secretory vesicles, depicting a general\n mechanism for vesicle fusion.}},\nDOI = {{10.3390/cells7120276}},\nArticle-Number = {{276}},\nEISSN = {{2073-4409}},\nResearcherID-Numbers = {{Mola, Maria Grazia/I-3507-2019\n BARBERI, Riccardo Cristoforo/D-9219-2012\n Mastrodonato, Maria/P-4513-2016\n }},\nORCID-Numbers = {{Mola, Maria Grazia/0000-0002-4421-9237\n NICOTERA, Isabella/0000-0002-4411-0573\n BARBERI, Riccardo Cristoforo/0000-0001-9713-1696\n Mastrodonato, Maria/0000-0002-0799-8032\n FORMOSO, Vincenzo/0000-0003-4887-4893}},\nUnique-ID = {{ISI:000455320700054}},\n}\n\n","author_short":["Centrone, M.","De Santo, M. P.","Nicotera, I.","Labate, C.","Ranieri, M.","Di Mise, A.","Mola, M. 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