Home LiteratureArticle Details
PMID: 12573443 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Review

The OSBP-related proteins: a novel protein family involved in vesicle transport, cellular lipid metabolism, and cell signalling.

Biochimica et biophysica acta ·Vol. 1631 ·No. 1 ·2003-02-20 ·Pages 1-11

Lehto M, Olkkonen VM

Abstract

Proteins/genes showing high sequence homology to the mammalian oxysterol binding protein (OSBP) have been identified in a variety of eukaryotic organisms from yeast to man. The unifying feature of the gene products denoted as OSBP-related proteins (ORPs) is the presence of an OSBP-type ligand binding (LB) domain. The LB domains of OSBP and its closest homologue bind oxysterols, while data on certain other family members suggest interaction with phospholipids. Many ORPs also have a pleckstrin homology (PH) domain in the amino-terminal region. The PH domains of the family members studied in detail are known to interact with membrane phosphoinositides and play an important role in the intracellular targeting of the proteins. It is plausible that the ORPs constitute a regulatory apparatus that senses the status of specific lipid ligands in membranes, using the PH and/or LB domains, and mediates information to yet poorly known downstream machineries. Functional studies carried out on the ORP proteins in different organisms indicate roles of the gene family in diverse cellular processes including control of lipid metabolism, regulation of vesicle transport, and cell signalling events.

MeSH Terms
Biological Transport Carrier Proteins/chemistry,metabolism Consensus Sequence Humans Lipid Metabolism Protein Structure, Tertiary Protein Subunits RNA, Messenger/metabolism Receptors, Steroid/chemistry,genetics,metabolism Saccharomyces cerevisiae Sequence Homology Signal Transduction
Chemicals
Carrier Proteins Protein Subunits RNA, Messenger Receptors, Steroid oxysterol binding protein
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lehto Markku
Department of Molecular Medicine, National Public Health Institute, Biomedicum, PO Box 104, Haartmaninkatu 8, FIN-00251, Helsinki, Finland.
Olkkonen Vesa M
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
2003-02-20
Pages
1-11
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Corrections
ErratumIn
-
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com