scholarly journals Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands

1999 ◽  
Vol 96 (2) ◽  
pp. 511-516 ◽  
Author(s):  
K. Morita ◽  
M. Furuse ◽  
K. Fujimoto ◽  
S. Tsukita
Keyword(s):  
Tight Junction ◽  
Multigene Family ◽  
Transmembrane Domain ◽  
Domain Protein ◽  
Protein Components

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.

Dynamic changes in protein components of the tight junction during liver regeneration

2001 ◽  
Vol 305 (3) ◽  
pp. 399-409 ◽  
Author(s):  
Yasuyuki Takaki ◽  
Syu-ichi Hirai ◽  
Naoyuki Manabe ◽  
Yasushi Izumi ◽  
Tomonori Hirose ◽  
...  
Keyword(s):  
Tight Junction ◽  
Liver Regeneration ◽  
Dynamic Changes ◽  
Protein Components

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.

Occludin TM4-: an isoform of the tight junction protein present in primates lacking the fourth transmembrane domain

2002 ◽  
Vol 115 (15) ◽  
pp. 3171-3180
Author(s):  
M. Reza Ghassemifar ◽  
Bhavwanti Sheth ◽  
Tom Papenbrock ◽  
Henry J. Leese ◽  
Franchesca D. Houghton ◽  
...  
Keyword(s):  
Tight Junction ◽  
Transmembrane Domain ◽  
Tight Junction Protein ◽  
Pcr Analysis ◽  
Weak Band ◽  
Reading Frame ◽  
Reverse Transcription Pcr ◽  
C Terminus ◽  
Junction Protein ◽  
Exon 4

The tight junction protein occludin possesses four transmembrane domains,two extracellular loops, and cytoplasmic N- and C-termini. Reverse transcription-PCR analysis of human tissues, embryos and cells using primers spanning the fourth transmembrane domain (TM4) and adjacent C-terminal region revealed two products. The larger and predominant product corresponded in sequence to canonical occludin (TM4+), while the smaller product exhibited a 162 bp deletion encoding the entire TM4 and immediate C-terminal flanking region (TM4-). Examination of the genomic occludin sequence identified that the 162 bp sequence deleted in TM4-coincided precisely with occludin exon 4, strongly suggesting that TM4- is an alternative splice isoform generated by skipping of exon 4. Indeed, the reading frame of downstream exons is not affected by exclusion of exon 4. The presence of both TM4+ and TM4- occludin isoforms was also identified in monkey epithelial cells but TM4-was undetected in murine and canine tissue and cells, indicating a late evolutionary origin for this alternative splicing event. Conceptual translation of TM4- isoform predicts extracellular localisation of the C-terminus. Immunocytochemical processing of living human Caco-2 cells using a C-terminal occludin antibody revealed weak, discontinuous staining restricted to the periphery of subconfluent islands of cells, or islands generated by wounding confluent layers. In occludin immunoblots, a weak band at ∼58 kDa, smaller than the predominant band at 65 kDa and corresponding to the predicted mass of TM4- isoform, is evident and upregulated in subconfluent cells. These data suggest that the TM4- isoform may be translated at low levels in specific conditions and may contribute to regulation of occludin function.

scholarly journals Multiple Protein Interactions Involving Proposed Extracellular Loop Domains of the Tight Junction Protein Occludin

2005 ◽  
Vol 16 (4) ◽  
pp. 1725-1734 ◽  
Author(s):  
Asma Nusrat ◽  
G. Thomas Brown ◽  
Jeffrey Tom ◽  
Alex Drake ◽  
Tam T.T. Bui ◽  
...  
Keyword(s):  
Tight Junction ◽  
Protein Interactions ◽  
Integral Membrane Protein ◽  
Intestinal Cell ◽  
Intestinal Cell Line ◽  
Multiple Protein ◽  
Junction Protein ◽  
Central Regions ◽  
Protein Components ◽  
Endothelial Tight Junction

Occludin is a tetraspan integral membrane protein in epithelial and endothelial tight junction (TJ) structures that is projected to have two extracellular loops. We have used peptides emulating central regions of human occludin's first and second loops, termed O-A:101–121 and O-B:210–228, respectively, to examine potential molecular interactions between these two regions of occludin and other TJ proteins. A superficial biophysical assessment of A:101–121 and O-B:210–228 showed them to have dissimilar solution conformation characteristics. Although O-A:101–121 failed to strongly interact with protein components of the human epithelial intestinal cell line T84, O-B:210–228 selectively associated with occludin, claudin-one and the junctional adhesion molecule (JAM)-A. Further, the presence of O-B:210–228, but not O-A:101–121, impeded the recovery of functional TJ structures. A scrambled peptide sequences of O-B:210–228 failed to influence TJ assembly. These studies demonstrate distinct properties for these two extracellular segments of the occludin protein and provide an improved understanding of how specific domains of occludin may interact with proteins present at TJ structures.

scholarly journals The Coxsackievirus and Adenovirus Receptor Interacts with the Multi-PDZ Domain Protein-1 (MUPP-1) within the Tight Junction

2004 ◽  
Vol 279 (46) ◽  
pp. 48079-48084 ◽  
Author(s):  
Carolyn B. Coyne ◽  
Tauni Voelker ◽  
Susan L. Pichla ◽  
Jeffrey M. Bergelson
Keyword(s):  
Tight Junction ◽  
Pdz Domain ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Domain Protein ◽  
Adenovirus Receptor

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
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