Structure and function of a model member of the SulP transporter family

Patrick Loughlin; Megan C. Shelden; M. Louise Tierney; Susan M. Howitt

doi:10.1385/CBB:36:2-3:183

Structure and function of a model member of the SulP transporter family

Patrick Loughlin, Megan C. Shelden, M. Louise Tierney, Susan M. Howitt^*

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

14 Citations (Scopus)

Abstract

SHST1 is a sulfate transporter that belongs to a large and diverse family of anion transporters. Little is known about the structure and function of any member of the family. Site-directed mutagenesis of SHST1 is being used to understand the function of particular amino acids. We have mutated highly conserved amino acid residues and the results suggest that the first two helices play an important role in the transport pathway. Furthermore, mutation of equivalent residues to those altered in human genetic diseases produces deleterious effects in SHST1. These results suggest that there are similarities in the molecular mechanism of transport throughout the family and the information obtained with SHST1 may be applicable to the entire family.

Original language	English
Pages (from-to)	183-190
Number of pages	8
Journal	Cell Biochemistry and Biophysics
Volume	36
Issue number	2-3
DOIs	https://doi.org/10.1385/CBB:36:2-3:183
Publication status	Published - 2002

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title = "Structure and function of a model member of the SulP transporter family",

abstract = "SHST1 is a sulfate transporter that belongs to a large and diverse family of anion transporters. Little is known about the structure and function of any member of the family. Site-directed mutagenesis of SHST1 is being used to understand the function of particular amino acids. We have mutated highly conserved amino acid residues and the results suggest that the first two helices play an important role in the transport pathway. Furthermore, mutation of equivalent residues to those altered in human genetic diseases produces deleterious effects in SHST1. These results suggest that there are similarities in the molecular mechanism of transport throughout the family and the information obtained with SHST1 may be applicable to the entire family.",

keywords = "Congenital chloride diarrhea, Diastrophic dysplasia, Pendrin, Prestin, Site-directed mutagenesis, Sulfate transporter, Transmembrane helix",

author = "Patrick Loughlin and Shelden, {Megan C.} and Tierney, {M. Louise} and Howitt, {Susan M.}",

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AU - Loughlin, Patrick

AU - Shelden, Megan C.

AU - Tierney, M. Louise

AU - Howitt, Susan M.

PY - 2002

Y1 - 2002

N2 - SHST1 is a sulfate transporter that belongs to a large and diverse family of anion transporters. Little is known about the structure and function of any member of the family. Site-directed mutagenesis of SHST1 is being used to understand the function of particular amino acids. We have mutated highly conserved amino acid residues and the results suggest that the first two helices play an important role in the transport pathway. Furthermore, mutation of equivalent residues to those altered in human genetic diseases produces deleterious effects in SHST1. These results suggest that there are similarities in the molecular mechanism of transport throughout the family and the information obtained with SHST1 may be applicable to the entire family.

AB - SHST1 is a sulfate transporter that belongs to a large and diverse family of anion transporters. Little is known about the structure and function of any member of the family. Site-directed mutagenesis of SHST1 is being used to understand the function of particular amino acids. We have mutated highly conserved amino acid residues and the results suggest that the first two helices play an important role in the transport pathway. Furthermore, mutation of equivalent residues to those altered in human genetic diseases produces deleterious effects in SHST1. These results suggest that there are similarities in the molecular mechanism of transport throughout the family and the information obtained with SHST1 may be applicable to the entire family.

KW - Congenital chloride diarrhea

KW - Diastrophic dysplasia

KW - Pendrin

KW - Prestin

KW - Site-directed mutagenesis

KW - Sulfate transporter

KW - Transmembrane helix

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U2 - 10.1385/CBB:36:2-3:183

DO - 10.1385/CBB:36:2-3:183

M3 - Review article

SN - 1085-9195

VL - 36

SP - 183

EP - 190

JO - Cell Biochemistry and Biophysics

JF - Cell Biochemistry and Biophysics

IS - 2-3

ER -

Structure and function of a model member of the SulP transporter family

Abstract

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