Discontinuous membrane helices in transport proteins and their correlation with function

Screpanti, Emanuela; Hunte, Carola

doi:10.1016/j.jsb.2007.01.011

Cited by 135 publications

(78 citation statements)

References 34 publications

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“…Similar structural motifs are also found in the 3-D structures of transporters with known structure, e.g. (Forrest et al;Screpanti and Hunte, 2007), which underscore their role in substrate coordination. All SLC34 proteins, including bacterial homologs, are expected to have similar functional core elements comprising TMDs2-10 ( Fig.…”

Section: Structure-function Relationships Of Slc34 Proteinssupporting

confidence: 62%

Phosphate transporters of the SLC20 and SLC34 families

Forster

Hernando

Biber

et al. 2013

Molecular Aspects of Medicine

188

198

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Transport of inorganic phosphate (Pi) across the plasma membrane is essential for normal cellular function. Members of two families of SLC proteins (SLC20 and SLC34) act as Na(+)-dependent, secondary-active cotransporters to transport Pi across cell membranes. The SLC34 proteins are expressed in specific organs important for Pi homeostasis: NaPi-IIa (SLC34A1) and NaPi-IIc (SLC34A3) fulfill essential roles in Pi reabsorption in the kidney proximal tubule and NaPi-IIb (SLC34A2) mediates Pi absorption in the gut. The SLC20 proteins, PiT-1 (SLC20A1), PiT-2 (SLC20A2) are expressed ubiquitously in all tissues and although generally considered as "housekeeping" transport proteins, the discovery of tissue-specific activity, regulatory pathways and gene-related pathophysiologies, is redefining their importance. This review summarizes our current knowledge of SLC20 and SLC34 proteins in terms of their basic molecular characteristics, physiological roles, known pathophysiology and pharmacology. AbstractTransport of inorganic phosphate (P i ) across the plasma membrane is essential for normal cellular function. Members of two families of SLC proteins (SLC20 and SLC34) act as Na + -dependent, secondary-active cotransporters to transport P i across cell membranes. The SLC34 proteins are expressed in specific organs important for P i homeostasis: NaPi-IIa (SLC34A1) and NaPi-IIc (SLC34A3) fulfill essential roles in P i reabsorption in the kidney proximal tubule and NaPi-IIb (SLC34A2) mediates P i absorption in the gut. The SLC20 proteins, PiT-1 (SLC20A1), PiT-2 (SLC20A2) are expressed ubiquitously in all tissues and although generally considered as "housekeeping" transport proteins, the discovery of tissue-specific activity,regulatory pathways and gene-related pathophysiologies, is redefining their importance. This review summarises our current knowledge of SLC20 and SLC34 proteins in terms of their basic molecular characteristics, physiological roles, known pathophysiologies and pharmacology.3

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Section: Structure-function Relationships Of Slc34 Proteinssupporting

confidence: 62%

Phosphate transporters of the SLC20 and SLC34 families

Forster

Hernando

Biber

et al. 2013

Molecular Aspects of Medicine

188

198

View full text Add to dashboard Cite

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“…Such elements should be stabilized by interacting with adjacent residues, transported substrates (e.g. dehydrated cations), or by mediating alternate conformation rearrangements (44,54). Our data indicate that interactions with Me 2ϩ and/or H ϩ may stabilize SLC11 TMS1 Asp and TMS6 His.…”

Section: Discussionmentioning

confidence: 82%

“…These two motifs in anti-parallel orientation ((DPG) and ("HPM")) form a pair of extended peptides interrupting TMS1 and TMS6. Similar pairs of discontinuous helices (␣-helix-extended peptide-␣-helix) constitute a salient feature in five cation transporter structures, and pairs of antiparallel discontinuous TM helices may be part of a fold shared by several cation transporter families (54).…”

Section: Discussionmentioning

confidence: 99%

Solute Carrier 11 Cation Symport Requires Distinct Residues in Transmembrane Helices 1 and 6

Courville

Urbánková

Rensing

et al. 2008

Journal of Biological Chemistry

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“…Pairs of discontinuous helices play a key structure-functional role in this architecture [36]. These can be either transmembrane spanning, as found in…”

Section: Discussionmentioning

confidence: 99%