Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
 
 
DownloadE-Mail
 Lokale TagsFreigabegeschichteDetailsÜbersicht
  Structural domains required for channel function of the mouse transient receptor potential protein homologue TRP1β

Engelke, M., Friedrich, O., Budde, P., Schäfer, C., Niemann, U., Zitt, C., et al. (2002). Structural domains required for channel function of the mouse transient receptor potential protein homologue TRP1β. FEBS Letters, 523(1-3): 1, pp. 193-199. Retrieved from http://dx.doi.org/10.1016/S0014-5793(02)02971-X.

Item is

 

einblenden: alle ausblenden: alle

Basisdaten

einblenden: ausblenden:
Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0014-0E3B-A Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-0014-0E3C-8
Genre: Zeitschriftenartikel
Alternativer Titel : FEBS Lett.

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Engelke, Michael, Autor
Friedrich, Olaf, Autor
Budde, Petra, Autor
Schäfer, Christina, Autor
Niemann, Ursula, Autor
Zitt, Christof, Autor
Jüngling, Eberhard, Autor
Rocks, Oliver1, Autor
Lückhoff, Andreas, Autor
Frey, Jürgen, Autor
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              

Inhalt

einblenden:
ausblenden:
Schlagwörter: transient receptor potential protein; coiled-coil domain; ankyrin-like repeat; HEK293 cell; patch clamp; yeast two-hybrid system
 Zusammenfassung: Transient receptor potential proteins (TRP) are supposed to participate in the formation of store-operated Ca2+ influx channels by co-assembly. However, little is known which domains facilitate the interaction of subunits. Contribution of the N- terminal coiled-coil domain and ankyrin-like repeats and the putative pore region of the mouse TRP1beta (mTRP1beta) variant to the formation of functional cation channels were analyzed following overexpression in HEK293 (human embryonic kidney) cells. MTRP1beta expressing cells exhibited enhanced Ca2+ influx and enhanced whole-cell membrane currents compared to mTRP1beta deletion mutants. Using a yeast two-hybrid assay only the coiled-coil domain facilitated homodimerization of the N- terminus. These results suggest that the N-terminus of mTRP1beta is required for structural organization thus forming functional channels. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2002-07-17
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 15402
URI: http://dx.doi.org/10.1016/S0014-5793(02)02971-X
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: FEBS Letters
  Alternativer Titel : FEBS Lett.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 523 (1-3) Artikelnummer: 1 Start- / Endseite: 193 - 199 Identifikator: -