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dc.contributor.author
Curcio Morelli, Cyntia
dc.contributor.author
Zhang, Peng
dc.contributor.author
Venugopal, Bhuvarahamurthy
dc.contributor.author
Charles, Florie A.
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Browning, Marsha F.
dc.contributor.author
Cantiello, Horacio Fabio
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dc.contributor.author
Slaugenhaupt, Susan A.
dc.date.available
2017-03-27T18:42:09Z
dc.date.issued
2010-02
dc.identifier.citation
Curcio Morelli, Cyntia; Zhang, Peng; Venugopal, Bhuvarahamurthy; Charles, Florie A.; Browning, Marsha F.; et al.; Functional multimerization of mucolipin channel proteins; Wiley; Journal of Cellular Physiology; 222; 2; 2-2010; 328-335
dc.identifier.issn
0021-9541
dc.identifier.uri
http://hdl.handle.net/11336/14281
dc.description.abstract
MCOLN1 encodes mucolipin-1 (TRPML1), a member of the transient receptor potential TRPML subfamily of channel proteins. Mutations in MCOLN1 cause mucolipidosis-type IV (MLIV), a lysosomal storage disorder characterized by severe neurologic, ophthalmologic, and gastrointestinal abnormalities. Along with TRPML1, there are two other TRPML family members, mucolipin-2 (TRPML2) and mucolipin-3 (TRPML3). In this study, we used immunocytochemical analysis to determine that TRPML1, TRPML2, and TRPML3 co-localize in cells. The multimerization of TRPML proteins was confirmed by co-immunoprecipitation and Western blot analysis, which demonstrated that TRPML1 homo-multimerizes as well as hetero-multimerizes with TRPML2 and TRPML3. MLIV-causing mutants of TRPML1 also interacted with wild-type TRPML1. Lipid bilayer re-constitution of in vitro translated TRPML2 and TRPML3 confirmed their cation channel properties with lower single channel conductance and higher partial permeability to anions as compared to TRPML1. We further analyzed the electrophysiological properties of single channel TRPML hetero-multimers, which displayed functional differences when compared to individual TRPMLs. Our data shows for the first time that TRPMLs form distinct functional channel complexes. Homo- and hetero-multimerization of TRPMLs may modulate channel function and biophysical properties, thereby increasing TRPML functional diversity.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Ml1
dc.subject
Multimerization
dc.subject.classification
Otras Medicina Básica
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dc.subject.classification
Medicina Básica
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dc.subject.classification
CIENCIAS MÉDICAS Y DE LA SALUD
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dc.title
Functional multimerization of mucolipin channel proteins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-03-21T20:11:17Z
dc.identifier.eissn
1097-4652
dc.journal.volume
222
dc.journal.number
2
dc.journal.pagination
328-335
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Hoboken
dc.description.fil
Fil: Curcio Morelli, Cyntia. Harvard Medical School; Estados Unidos
dc.description.fil
Fil: Zhang, Peng. Massachusetts General Hospital East; Estados Unidos
dc.description.fil
Fil: Venugopal, Bhuvarahamurthy. Harvard Medical School; Estados Unidos
dc.description.fil
Fil: Charles, Florie A.. Harvard Medical School; Estados Unidos
dc.description.fil
Fil: Browning, Marsha F.. Harvard Medical School; Estados Unidos
dc.description.fil
Fil: Cantiello, Horacio Fabio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Massachusetts General Hospital East; Estados Unidos
dc.description.fil
Fil: Slaugenhaupt, Susan A.. Harvard Medical School; Estados Unidos
dc.journal.title
Journal of Cellular Physiology
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/jcp.21956/abstract
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/jcp.21956
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