Fatty acid transfer from Yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes

Sterol carrier protein 2 (SCP2) is an intracellular protein domain found in all forms of life. It was originally identified as a sterol transfer protein, but was recently shown to also bind phospholipids, fatty acids, and fatty-acyl-CoA with high affinity. Based on studies carried out in higher euka...

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Autores principales: Falomir Lockhart, Lisandro J., Burgardt, Noelia I., Ferreyra, Raúl G., Ceolín, Marcelo Raúl, Ermácora, Mario R., Córsico, Betina
Formato: Articulo
Lenguaje:Inglés
Publicado: 2009
Materias:
Biología
Fatty Acid
Sterol carrier protein 2
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/82703
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-82703
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Fatty Acid
Sterol carrier protein 2
spellingShingle Biología
Fatty Acid
Sterol carrier protein 2
Falomir Lockhart, Lisandro J.
Burgardt, Noelia I.
Ferreyra, Raúl G.
Ceolín, Marcelo Raúl
Ermácora, Mario R.
Córsico, Betina
Fatty acid transfer from Yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes
topic_facet Biología
Fatty Acid
Sterol carrier protein 2
description Sterol carrier protein 2 (SCP2) is an intracellular protein domain found in all forms of life. It was originally identified as a sterol transfer protein, but was recently shown to also bind phospholipids, fatty acids, and fatty-acyl-CoA with high affinity. Based on studies carried out in higher eukaryotes, it is believed that SCP2 targets its ligands to compartmentalized intracellular pools and participates in lipid traffic, signaling, and metabolism. However, the biological functions of SCP2 are incompletely characterized and may be different in microorganisms. Herein, we demonstrate the preferential localization of SCP2 of Yarrowia lipolytica (YLSCP2) in peroxisome-enriched fractions and examine the rate and mechanism of transfer of anthroyloxy fatty acid from YLSCP2 to a variety of phospholipid membranes using a fluorescence resonance energy transfer assay. The results show that fatty acids are transferred by a collision-mediated mechanism, and that negative charges on the membrane surface are important for establishing a "collisional complex". Phospholipids, which are major constituents of peroxisome and mitochondria, induce special effects on the rates of transfer. In conclusion, YLSCP2 may function as a fatty acid transporter with some degree of specificity, and probably diverts fatty acids to the peroxisomal metabolism.
format Articulo
Articulo
author Falomir Lockhart, Lisandro J.
Burgardt, Noelia I.
Ferreyra, Raúl G.
Ceolín, Marcelo Raúl
Ermácora, Mario R.
Córsico, Betina
author_facet Falomir Lockhart, Lisandro J.
Burgardt, Noelia I.
Ferreyra, Raúl G.
Ceolín, Marcelo Raúl
Ermácora, Mario R.
Córsico, Betina
author_sort Falomir Lockhart, Lisandro J.
title Fatty acid transfer from Yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes
title_short Fatty acid transfer from Yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes
title_full Fatty acid transfer from Yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes
title_fullStr Fatty acid transfer from Yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes
title_full_unstemmed Fatty acid transfer from Yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes
title_sort fatty acid transfer from yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes
publishDate 2009
url http://sedici.unlp.edu.ar/handle/10915/82703
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