scholarly journals USH3A transcripts encode clarin-1, a four-transmembrane-domain protein with a possible role in sensory synapses

2002 ◽  
Vol 10 (6) ◽  
pp. 339-350 ◽  
Author(s):  
Avital Adato ◽  
Sarah Vreugde ◽  
Tarja Joensuu ◽  
Nili Avidan ◽  
Riikka Hamalainen ◽  
...  
Keyword(s):  
Transmembrane Domain ◽  
Domain Protein

scholarly journals A family of rhomboid-like genes: Drosophila rhomboid-1 and roughoid/rhomboid-3 cooperate to activate EGF receptor signaling

2000 ◽  
Vol 14 (13) ◽  
pp. 1651-1663 ◽  
Author(s):  
Jonathan D. Wasserman ◽  
Sinisa Urban ◽  
Matthew Freeman
Keyword(s):  
Molecular Mechanism ◽  
Growth And Development ◽  
Egf Receptor ◽  
Transmembrane Domain ◽  
Large Family ◽  
Egfr Signaling ◽  
Apparent Lack ◽  
Cell Determination ◽  
Domain Protein ◽  
Rate Limiting

As in mammals, the Drosophila EGF receptor controls many aspects of growth and development. The rate limiting component ofDrosophila Egfr signaling is Rhomboid, a seven transmembrane domain protein, whose expression prefigures Egfr signaling. Little is known about the molecular mechanism of Rhomboid function but genetic evidence suggests that it controls the activation of the ligand Spitz, a TGFα-like factor. Spitz/Egfr signaling regulates cell determination in the eye but here there is no apparent function for Rhomboid, an observation that casts doubt on this prevailing model of Rhomboid function. We describe our identification of six newrhomboid-like genes in Drosophila, and a large family of related genes present in organisms as diverse as bacteria and mammals; a human rhomboid homolog has also recently been described. Drosophila rhomboid-3 corresponds to theroughoid mutation; it cooperates with rhomboid-1 to control Egfr signaling in the eye, thereby solving the puzzle of the apparent lack of Rhomboid-1 function there. Rhomboid-1 and Roughoid/Rhomboid-3 act in the signal-emitting not signal-receiving cell, supporting the idea that Spitz activation is regulated by Rhomboid-like molecules.

scholarly journals Peripheral Coupling Sites Formed by STIM1 Govern the Contractility of Vascular Smooth Muscle Cells

2021 ◽  
Author(s):  
Vivek Krishnan ◽  
Sher Ali ◽  
Albert L. Gonzales ◽  
Pratish Thakore ◽  
Caoimhin S. Griffin ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Transmembrane Domain ◽  
Muscle Cells ◽  
Channel Activity ◽  
Resistance Arteries ◽  
Store Depletion ◽  
Domain Protein

Peripheral coupling between the sarcoplasmic reticulum (SR) and plasma membrane (PM) forms signaling complexes that regulate the membrane potential and contractility of vascular smooth muscle cells (VSMCs), although the mechanisms responsible for these membrane interactions are poorly understood. In many cells, STIM1 (stromal interaction molecule 1), a single transmembrane-domain protein that resides in the endoplasmic reticulum (ER), transiently moves to ER-PM junctions in response to depletion of ER Ca2+ stores and initiates store-operated Ca2+ entry (SOCE). Fully differentiated VSMCs express STIM1 but exhibit only marginal SOCE activity. We hypothesized that STIM1 is constitutively active in contractile VSMCs and maintains peripheral coupling. In support of this concept, we found that the number and size of SR-PM interacting sites were decreased and SR-dependent Ca2+ signaling processes were disrupted in freshly isolated cerebral artery SMCs from tamoxifen-inducible, SMC specific STIM1-knockout (Stim1-smKO) mice. VSMCs from Stim1-smKO mice also exhibited a reduction in nanoscale colocalization between Ca2+-release sites on the SR and Ca2+-activated ion channels on the PM, accompanied by diminished channel activity. Stim1-smKO mice were hypotensive and resistance arteries isolated from them displayed blunted contractility. These data suggest that STIM1 – independent of SR Ca2+ store depletion – is critically important for stable peripheral coupling in contractile VSMCs.

scholarly journals Loss of Occludin Affects Tricellular Localization of Tricellulin

2008 ◽  
Vol 19 (11) ◽  
pp. 4687-4693 ◽  
Author(s):  
Junichi Ikenouchi ◽  
Hiroyuki Sasaki ◽  
Sachiko Tsukita ◽  
Mikio Furuse ◽  
Shoichiro Tsukita
Keyword(s):  
Plasma Membrane ◽  
Tight Junction ◽  
Tight Junctions ◽  
Molecular Mechanisms ◽  
Transmembrane Domain ◽  
Polarized Epithelia ◽  
Cross Links ◽  
Exogenous Expression ◽  
Domain Protein ◽  
Zona Occludens

The tricellular tight junction (tTJ) forms at the convergence of bicellular tight junctions (bTJs) where three epithelial cells meet in polarized epithelia, and it is required for the maintenance of the transepithelial barrier. Tricellulin is a four transmembrane domain protein recently identified as the first marker of tTJ, but little is known about how tricellulin is localized at tTJs. As for the molecular mechanism of association of tricellulin with tight junctions (TJs), we found that tricellulin was incorporated into claudin-based TJs independently of binding to zona occludens-1. Unexpectedly, exogenous expression of tricellulin increased cross-links of TJ strands in the plasma membrane. As for the molecular mechanisms for localization of tricellulin at tricellular junctions, we found that knockdown of occludin caused mislocalization of tricellulin to bTJs, implying that occludin supports tricellular localization of tricellulin by excluding tricellulin from bTJs.

Mutations in a Novel Gene, Encoding a Single Transmembrane Domain Protein Are Associated with Familial Glucocorticoid Deficiency Type 2

2004 ◽  
Vol 30 (4) ◽  
pp. 889-890 ◽  
Author(s):  
Louise A. Metherell ◽  
Sadani Cooray ◽  
Angela Huebner ◽  
Franz Ruschendorf ◽  
Danielle Naville ◽  
...  
Keyword(s):  
Transmembrane Domain ◽  
Gene Encoding ◽  
Novel Gene ◽  
Domain Protein ◽  
Glucocorticoid Deficiency ◽  
Deficiency Type

scholarly journals Cutting Edge: Chandra, a Novel Four-Transmembrane Domain Protein Differentially Expressed in Helper Type 1 Lymphocytes

2000 ◽  
Vol 165 (2) ◽  
pp. 632-636 ◽  
Author(s):  
Chandrasekar Venkataraman ◽  
Gabriele Schaefer ◽  
Ulrike Schindler
Keyword(s):  
Transmembrane Domain ◽  
Cutting Edge ◽  
Differentially Expressed ◽  
Domain Protein ◽  
Helper Type

Genomic structure and expression of Lestd1, a seven-transmembrane-domain protein- encoding gene specifically expressed in tomato pollen

2005 ◽  
Vol 53 (2) ◽  
pp. 79-88
Author(s):  
YEHIAM SALTS ◽  
IRINA SOBOLEV ◽  
INNA CHMELNITSKY ◽  
SARA SHABTAI ◽  
RIVKA BARG
Keyword(s):  
Transmembrane Domain ◽  
Genomic Structure ◽  
Protein Encoding ◽  
Domain Protein ◽  
Encoding Gene

scholarly journals The human CD53 gene, coding for a four transmembrane domain protein, maps to chromosomal region 1p13

Genomics ◽  
1993 ◽  
Vol 18 (3) ◽  
pp. 725-728 ◽  
Author(s):  
M. Eugenia Gonzalez ◽  
Fernando Pardo-Manuel de Villena ◽  
Elena Fernandez-Ruiz ◽  
Santiago Rodriguez de Cordoba ◽  
Pedro A. Lazo
Keyword(s):  
Chromosomal Region ◽  
Transmembrane Domain ◽  
Gene Coding ◽  
Domain Protein

scholarly journals Localization to Mature Melanosomes by Virtue of Cytoplasmic Dileucine Motifs Is Required for Human OCA2 Function

2009 ◽  
Vol 20 (5) ◽  
pp. 1464-1477 ◽  
Author(s):  
Anand Sitaram ◽  
Rosanna Piccirillo ◽  
Ilaria Palmisano ◽  
Dawn C. Harper ◽  
Esteban C. Dell'Angelica ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Steady State ◽  
Subcellular Localization ◽  
Transmembrane Domain ◽  
Pigment Cell ◽  
Oculocutaneous Albinism ◽  
Melanin Synthesis ◽  
Sorting Motif ◽  
Domain Protein

Oculocutaneous albinism type 2 is caused by defects in the gene OCA2, encoding a pigment cell-specific, 12-transmembrane domain protein with homology to ion permeases. The function of the OCA2 protein remains unknown, and its subcellular localization is under debate. Here, we show that endogenous OCA2 in melanocytic cells rapidly exits the endoplasmic reticulum (ER) and thus does not behave as a resident ER protein. Consistently, exogenously expressed OCA2 localizes within melanocytes to melanosomes, and, like other melanosomal proteins, localizes to lysosomes when expressed in nonpigment cells. Mutagenized OCA2 transgenes stimulate melanin synthesis in OCA2-deficient cells when localized to melanosomes but not when specifically retained in the ER, contradicting a proposed primary function for OCA2 in the ER. Steady-state melanosomal localization requires a conserved consensus acidic dileucine-based sorting motif within the cytoplasmic N-terminal region of OCA2. A second dileucine signal within this region confers steady-state lysosomal localization in melanocytes, suggesting that OCA2 might traverse multiple sequential or parallel trafficking routes. The two dileucine signals physically interact in a differential manner with cytoplasmic adaptors known to function in trafficking other proteins to melanosomes. We conclude that OCA2 is targeted to and functions within melanosomes but that residence within melanosomes may be regulated by secondary or alternative targeting to lysosomes.

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