The electroneutral cation-chloride cotransporters.

1998 ◽  
Vol 201 (14) ◽  
pp. 2091-2102 ◽  
Author(s):  
D B Mount ◽  
E Delpire ◽  
G Gamba ◽  
A E Hall ◽  
E Poch ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Gene Family ◽  
Molecular Identification ◽  
Membrane Topology ◽  
Cytoplasmic Domains ◽  
Transmembrane Segments ◽  
Novel Gene ◽  
Lower Eukaryotes ◽  
Homologous Genes ◽  
Cation Chloride Cotransporters

Electroneutral cation-chloride cotransporters are widely expressed and perform a variety of physiological roles. A novel gene family of five members, encompassing a Na+-Cl- transporter, two Na+-K+-2Cl- transporters and two K+-Cl- cotransporters, encodes these membrane proteins; homologous genes have also been identified in a prokaryote and a number of lower eukaryotes. The cotransporter proteins share a common predicted membrane topology, with twelve putative transmembrane segments flanked by long hydrophilic N- and C-terminal cytoplasmic domains. The molecular identification of these transporters has had a significant impact on the study of their function, regulation and pathophysiology.

scholarly journals Classes of non-conventional tetraspanins defined by alternative splicing

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Nikolas Hochheimer ◽  
Ricarda Sies ◽  
Anna C. Aschenbrenner ◽  
Dirk Schneider ◽  
Thorsten Lang
Keyword(s):  
Alternative Splicing ◽  
Membrane Proteins ◽  
Membrane Topology ◽  
Gene Products ◽  
Extracellular Loop ◽  
Transmembrane Topology ◽  
Transmembrane Segments ◽  
Structural Variability ◽  
Large Extracellular Loop

Abstract Tetraspanins emerge as a family of membrane proteins mediating an exceptional broad diversity of functions. The naming refers to their four transmembrane segments, which define the tetraspanins‘ typical membrane topology. In this study, we analyzed alternative splicing of tetraspanins. Besides isoforms with four transmembrane segments, most mRNA sequences are coding for isoforms with one, two or three transmembrane segments, representing structurally mono-, di- and trispanins. Moreover, alternative splicing may alter transmembrane topology, delete parts of the large extracellular loop, or generate alternative N- or C-termini. As a result, we define structure-based classes of non-conventional tetraspanins. The increase in gene products by alternative splicing is associated with an unexpected high structural variability of tetraspanins. We speculate that non-conventional tetraspanins have roles in regulating ER exit and modulating tetraspanin-enriched microdomain function.

scholarly journals Epithelial Membrane Protein-1, Peripheral Myelin Protein 22, and Lens Membrane Protein 20 Define a Novel Gene Family

1995 ◽  
Vol 270 (48) ◽  
pp. 28824-28833 ◽  
Author(s):  
Verdon Taylor ◽  
Andrew A. Welcher ◽  
EST Program Amgen ◽  
Ueli Suter
Keyword(s):  
Membrane Protein ◽  
Gene Family ◽  
Myelin Protein ◽  
Peripheral Myelin Protein 22 ◽  
Peripheral Myelin Protein ◽  
Novel Gene

scholarly journals Planarian cell number depends on blitzschnell, a novel gene family that balances cell proliferation and cell death

Development ◽  
2020 ◽  
Vol 147 (7) ◽  
pp. dev184044 ◽  
Author(s):  
Eudald Pascual-Carreras ◽  
Marta Marin-Barba ◽  
Carlos Herrera-Úbeda ◽  
Daniel Font-Martín ◽  
Kay Eckelt ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Cell Death ◽  
Gene Family ◽  
Cell Number ◽  
Novel Gene

scholarly journals Stability and flexibility of marginally hydrophobic–segment stalling at the endoplasmic reticulum translocon

2016 ◽  
Vol 27 (6) ◽  
pp. 930-940 ◽  
Author(s):  
Yuichiro Kida ◽  
Yudai Ishihara ◽  
Hidenobu Fujita ◽  
Yukiko Onishi ◽  
Masao Sakaguchi
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Lipid Phase ◽  
Endoplasmic Reticulum Membrane ◽  
Dependent Manner ◽  
Transmembrane Segment ◽  
Conducting Channel ◽  
Transmembrane Segments ◽  
Lipid Environment ◽  
Sec61 Channel

Many membrane proteins are integrated into the endoplasmic reticulum membrane through the protein-conducting channel, the translocon. Transmembrane segments with insufficient hydrophobicity for membrane integration are frequently found in multispanning membrane proteins, and such marginally hydrophobic (mH) segments should be accommodated, at least transiently, at the membrane. Here we investigated how mH-segments stall at the membrane and their stability. Our findings show that mH-segments can be retained at the membrane without moving into the lipid phase and that such segments flank Sec61α, the core channel of the translocon, in the translational intermediate state. The mH-segments are gradually transferred from the Sec61 channel to the lipid environment in a hydrophobicity-dependent manner, and this lateral movement may be affected by the ribosome. In addition, stalling mH-segments allow for insertion of the following transmembrane segment, forming an Ncytosol/Clumen orientation, suggesting that mH-segments can move laterally to accommodate the next transmembrane segment. These findings suggest that mH-segments may be accommodated at the ER membrane with lateral fluctuation between the Sec61 channel and the lipid phase.

scholarly journals GRIF-1 and OIP106, Members of a Novel Gene Family of Coiled-Coil Domain Proteins

2005 ◽  
Vol 280 (15) ◽  
pp. 14723-14732 ◽  
Author(s):  
Kieran Brickley ◽  
Miriam J. Smith ◽  
Mike Beck ◽  
F. Anne Stephenson
Keyword(s):  
Gene Family ◽  
Coiled Coil ◽  
Novel Gene ◽  
Coiled Coil Domain
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