Mammalian farnesyltransferase α subunit regulates vacuolar protein sorting-associated protein 4A (Vps4A)--dependent intracellular trafficking through recycling endosomes.
Biochem Biophys Res Commun
; 468(4): 580-6, 2015 Dec 25.
Article
en En
| MEDLINE
| ID: mdl-26551458
ABSTRACT
The protein farnesyltransferase (FTase) mediates posttranslational modification of proteins with isoprenoid lipids. FTase is a heterodimer and although the ß subunit harbors the active site, it requires the α subunit for its activity. Here we explore the other functions of the FTase α subunit in addition to its established role in protein prenylation. We found that in the absence of the ß subunit, the α subunit of FTase forms a stable autonomous dimeric structure in solution. We identify interactors of FTase α using mass spectrometry, followed by rapid in vitro analysis using the Leishmania tarentolae cell - free system. Vps4A was validated for direct binding to the FTase α subunit both in vitro and in vivo. Analysis of the interaction with Vps4A in Hek 293 cells demonstrated that FTase α controls trafficking of transferrin receptor upstream of this protein. These results point to the existence of previously undetected biological functions of the FTase α subunit that includes control of intracellular membrane trafficking.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Endosomas
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Fracciones Subcelulares
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Adenosina Trifosfatasas
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Transporte de Proteínas
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Endocitosis
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Farnesiltransferasa
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Complejos de Clasificación Endosomal Requeridos para el Transporte
Tipo de estudio:
Risk_factors_studies
Límite:
Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2015
Tipo del documento:
Article
País de afiliación:
Australia