Oligomerization of human ATP-binding cassette transporters and its potential significance in human disease

Wei Mo, Jian-Ting Zhang

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Human ATP-binding cassette transporters (ABC transporter) belong to an extremely important superfamily of membrane transporters. They use energy from ATP hydrolysis to transport a wide variety of substrates across the cellular membrane. Due to the physiological and pharmacological importance of their diverse substrates, ABC transporters have been shown to have close relationship with various human diseases such as cystic fibrosis and multi-drug resistance in cancer chemotherapy. While it has been thought traditionally that functional ABC transporters exist as monomeric full or dimeric half transporters, emerging evidence indicates that some ABC transporters oligomerize on cellular membranes and this oligomerization seems to have functional relevance. Therefore, this oligomerization process might be a promising drug target for ABC transporter-related human diseases, especially in overcoming multi-drug resistance in cancer chemotherapy. In this review, we perform a critical analysis of the past studies on the oligomerization of ABC transporters.

Original languageEnglish
Pages (from-to)1049-1063
Number of pages15
JournalExpert Opinion on Drug Metabolism and Toxicology
Volume5
Issue number9
DOIs
StatePublished - Sep 2009

Fingerprint

Oligomerization
ATP-Binding Cassette Transporters
Chemotherapy
Multiple Drug Resistance
Pharmaceutical Preparations
Membranes
Drug Therapy
Membrane Transport Proteins
Substrates
Cystic Fibrosis
Hydrolysis
Neoplasms
Adenosine Triphosphate
Pharmacology

Keywords

  • ABC transporter
  • Dimers
  • Multi-drug resistance
  • Oligomerization

ASJC Scopus subject areas

  • Toxicology
  • Pharmacology

Cite this

Oligomerization of human ATP-binding cassette transporters and its potential significance in human disease. / Mo, Wei; Zhang, Jian-Ting.

In: Expert Opinion on Drug Metabolism and Toxicology, Vol. 5, No. 9, 09.2009, p. 1049-1063.

Research output: Contribution to journalArticle

@article{1dfebcb1914446cc9fefc4e7dd5289cc,
title = "Oligomerization of human ATP-binding cassette transporters and its potential significance in human disease",
abstract = "Human ATP-binding cassette transporters (ABC transporter) belong to an extremely important superfamily of membrane transporters. They use energy from ATP hydrolysis to transport a wide variety of substrates across the cellular membrane. Due to the physiological and pharmacological importance of their diverse substrates, ABC transporters have been shown to have close relationship with various human diseases such as cystic fibrosis and multi-drug resistance in cancer chemotherapy. While it has been thought traditionally that functional ABC transporters exist as monomeric full or dimeric half transporters, emerging evidence indicates that some ABC transporters oligomerize on cellular membranes and this oligomerization seems to have functional relevance. Therefore, this oligomerization process might be a promising drug target for ABC transporter-related human diseases, especially in overcoming multi-drug resistance in cancer chemotherapy. In this review, we perform a critical analysis of the past studies on the oligomerization of ABC transporters.",
keywords = "ABC transporter, Dimers, Multi-drug resistance, Oligomerization",
author = "Wei Mo and Jian-Ting Zhang",
year = "2009",
month = "9",
doi = "10.1517/17425250903124371",
language = "English",
volume = "5",
pages = "1049--1063",
journal = "Expert Opinion on Drug Metabolism and Toxicology",
issn = "1742-5255",
publisher = "Informa Healthcare",
number = "9",

}

TY - JOUR

T1 - Oligomerization of human ATP-binding cassette transporters and its potential significance in human disease

AU - Mo, Wei

AU - Zhang, Jian-Ting

PY - 2009/9

Y1 - 2009/9

N2 - Human ATP-binding cassette transporters (ABC transporter) belong to an extremely important superfamily of membrane transporters. They use energy from ATP hydrolysis to transport a wide variety of substrates across the cellular membrane. Due to the physiological and pharmacological importance of their diverse substrates, ABC transporters have been shown to have close relationship with various human diseases such as cystic fibrosis and multi-drug resistance in cancer chemotherapy. While it has been thought traditionally that functional ABC transporters exist as monomeric full or dimeric half transporters, emerging evidence indicates that some ABC transporters oligomerize on cellular membranes and this oligomerization seems to have functional relevance. Therefore, this oligomerization process might be a promising drug target for ABC transporter-related human diseases, especially in overcoming multi-drug resistance in cancer chemotherapy. In this review, we perform a critical analysis of the past studies on the oligomerization of ABC transporters.

AB - Human ATP-binding cassette transporters (ABC transporter) belong to an extremely important superfamily of membrane transporters. They use energy from ATP hydrolysis to transport a wide variety of substrates across the cellular membrane. Due to the physiological and pharmacological importance of their diverse substrates, ABC transporters have been shown to have close relationship with various human diseases such as cystic fibrosis and multi-drug resistance in cancer chemotherapy. While it has been thought traditionally that functional ABC transporters exist as monomeric full or dimeric half transporters, emerging evidence indicates that some ABC transporters oligomerize on cellular membranes and this oligomerization seems to have functional relevance. Therefore, this oligomerization process might be a promising drug target for ABC transporter-related human diseases, especially in overcoming multi-drug resistance in cancer chemotherapy. In this review, we perform a critical analysis of the past studies on the oligomerization of ABC transporters.

KW - ABC transporter

KW - Dimers

KW - Multi-drug resistance

KW - Oligomerization

UR - http://www.scopus.com/inward/record.url?scp=70249099233&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=70249099233&partnerID=8YFLogxK

U2 - 10.1517/17425250903124371

DO - 10.1517/17425250903124371

M3 - Article

VL - 5

SP - 1049

EP - 1063

JO - Expert Opinion on Drug Metabolism and Toxicology

JF - Expert Opinion on Drug Metabolism and Toxicology

SN - 1742-5255

IS - 9

ER -