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BBA - Biomembranes (v.1778, #3)

Editorial Board (pp. ii).

Preface: The apical junctional complexes, composition, structure, and characteristics by Jean-Claude Hervé (pp. 559-561).

Molecular components of the adherens junction by Carien M. Niessen; Cara J. Gottardi (pp. 562-571).

Adherens junctions serve to couple individual cells into various arrangements required for tissue structure and function. The central structural components of adherens junctions are transmembrane adhesion receptors, and their associated actin-binding/regulatory proteins. The molecular machineries that organize these adhesion receptor complexes into higher order junction structures, and the functional consequences of this junctional organization will be discussed.

Keywords: Zonula adherens; Cadherin; Catenin; Nectin; Adhesion

Desmosome structure, composition and function by David Garrod; Martyn Chidgey (pp. 572-587).

Desmosomes are intercellular junctions of epithelia and cardiac muscle. They resist mechanical stress because they adopt a strongly adhesive state in which they are said to be hyper-adhesive and which distinguishes them from other intercellular junctions; desmosomes are specialised for strong adhesion and their failure can result in diseases of the skin and heart. They are also dynamic structures whose adhesiveness can switch between high and low affinity adhesive states during processes such as embryonic development and wound healing, the switching being signalled by protein kinase C. Desmosomes may also act as signalling centres, regulating the availability of signalling molecules and thereby participating in fundamental processes such as cell proliferation, differentiation and morphogenesis. Here we consider the structure, composition and function of desmosomes, and their role in embryonic development and disease.

Transmembrane proteins of tight junctions by Hideki Chiba; Makoto Osanai; Masaki Murata; Takashi Kojima; Norimasa Sawada (pp. 588-600).

Tight junctions contribute to the paracellular barrier, the fence dividing plasma membranes, and signal transduction, acting as a multifunctional complex in vertebrate epithelial and endothelial cells. The identification and characterization of the transmembrane proteins of tight junctions, claudins, junctional adhesion molecules (JAMs), occludin and tricellulin, have led to insights into the molecular nature of tight junctions. We provide an overview of recent progress in studies on these proteins and highlight their roles and regulation, as well as their functional significance in human diseases.

Keywords: Tight junction; Cell junction; Cell polarity; Claudin; Occludin; Junctional adhesion molecule

The cytoplasmic plaque of tight junctions: A scaffolding and signalling center by Laurent Guillemot; Serge Paschoud; Pamela Pulimeno; Andrea Foglia; Sandra Citi (pp. 601-613).

The region of cytoplasm underlying the tight junction (TJ) contains several multimolecular protein complexes, which are involved in scaffolding of membrane proteins, regulation of cytoskeletal organization, establishment of polarity, and signalling to and from the nucleus. In this review, we summarize some of the most recent advances in understanding the identity of these proteins, their domain organization, their protein interactions, and their functions in vertebrate organisms. Analysis of knockdown and knockout model systems shows that several TJ proteins are essential for the formation of epithelial tissues and early embryonic development, whereas others appear to have redundant functions.

Keywords: Tight junctions; Cytoplasmic proteins; ZO-1; ZO-2; ZO-3; MAGI; Afadin; MUPP1; Angiomotin; Cingulin; JACOP; Symplekin; ASH1; Ubinuclein; GEF-H1; Rich1; Tuba; Rab13; Rab3B; PDZ; PAR-3; PAR-6; PALS-1; PATJ

Polarity complex proteins by Emeline Assémat; Elsa Bazellières; Emilie Pallesi-Pocachard; André Le Bivic; Dominique Massey-Harroche (pp. 614-630).

The formation of functional epithelial tissues involves the coordinated action of several protein complexes, which together produce a cell polarity axis and develop cell–cell junctions. During the last decade, the notion of polarity complexes emerged as the result of genetic studies in which a set of genes was discovered first in Caenorhabditis elegans and then in Drosophila melanogaster. In epithelial cells, these complexes are responsible for the development of the apico-basal axis and for the construction and maintenance of apical junctions. In this review, we focus on apical polarity complexes, namely the PAR3/PAR6/aPKC complex and the CRUMBS/PALS1/PATJ complex, which are conserved between species and along with a lateral complex, the SCRIBBLE/DLG/LGL complex, are crucial to the formation of apical junctions such as tight junctions in mammalian epithelial cells. The exact mechanisms underlying their tight junction construction and maintenance activities are poorly understood, and it is proposed to focus in this review on establishing how these apical polarity complexes might regulate epithelial cell morphogenesis and functions. In particular, we will present the latest findings on how these complexes regulate epithelial homeostasis.

Keywords: Abbreviations; 5-HTR; serotonin receptor; Amot; angiomotin; APC; adenomatous polyposis coli; aPKC; atypical protein kinase C; CAR; Coxsackievirus and adenovirus receptor; CASK; calmodulin associated ser/thr kinase; C-kit; proto-oncogene (receptor for stem cell factor); CRB; crumbs; CRIB; Cdc42 Rac interaction binding; DLG; discs large; EMP55; 55-kDa erythrocyte membrane protein (p55); EPB41L5; erythrocyte protein band 4.1-like 5; EST; expressed sequence tag; FERM; band 4.1 ezrin radixin moesin; Has; heart and soul; HURP; hepatoma upregulated protein; InaD-like; inactivation no after-potential D; JAM; junctional adhesion molecule; K; chromosome; L27; Lin2 lin7; LAP; LRR and PDZ; LGL; lethal giant larvae; LRR; leucine-rich repeats; MAGUK; membrane-associated guanylate kinase; MOE; mosaic eyes; MPP; membrane protein palmitoylated; MUPP1; multi PDZ domain protein; MW; molecular weight; NG2; membrane-spanning proteoglycan; NOK; Nagie oko protein; Ome; oko meduzy; PALS; proteins associated with Lin seven; PAR; partition defective; PATJ; protein-associated with tight junction; PDZ; PSD-95, discs large, ZO-1; PI3K; phoshoinositide 3-kinase; PTEN; protein tyrosin phosphatase and tensin homologue; SAP102; synapse-associated protein 102; SCRIB; scribble; Sdt; stardust; SH3; Src homology domain 3; TAPP; tandem-PH (pleckstrin-homology)-domain-containing protein; TARPs; transmembrane AMPA receptor regulated proteins; TSC; tuberous sclerosis complex; TSHR; thyroid stimulating hormone receptor; VAM; veli-associated MAGUK; YMO; yurt mosaic eyes like; ZO; zonula occludensTight junction; Epithelium; PAR complex; CRUMBS complex; SCRIBBLE complex

Structure and function of claudins by Gerd Krause; Lars Winkler; Sebastian L. Mueller; Reiner F. Haseloff; Jörg Piontek; Ingolf E. Blasig (pp. 631-645).

Claudins are tetraspan transmembrane proteins of tight junctions. They determine the barrier properties of this type of cell–cell contact existing between the plasma membranes of two neighbouring cells, such as occurring in endothelia or epithelia. Claudins can completely tighten the paracellular cleft for solutes, and they can form paracellular ion pores. It is assumed that the extracellular loops specify these claudin functions. It is hypothesised that the larger first extracellular loop is critical for determining the paracellular tightness and the selective ion permeability. The shorter second extracellular loop may cause narrowing of the paracellular cleft and have a holding function between the opposing cell membranes. Sequence analysis of claudins has led to differentiation into two groups, designated as classic claudins (1–10, 14, 15, 17, 19) and non-classic claudins (11–13, 16, 18, 20–24), according to their degree of sequence similarity. This is also reflected in the derived sequence-structure function relationships for extracellular loops 1 and 2. The concepts evolved from these findings and first tentative molecular models for homophilic interactions may explain the different functional contribution of the two extracellular loops at tight junctions.

Keywords: Tight junction; Transmembrane protein; Claudin; Extracellular loop; Cell–cell contact; Paracellular pore; Structural model; Epithelial and endothelial barriers

Structural organization of the tight junctions by Luca Paris; Laura Tonutti; Cristina Vannini; Gianfranco Bazzoni (pp. 646-659).

Tight junctions are the most apical organelle of the apical junctional complex and are primarily involved in the regulation of paracellular permeability and membrane polarity. Extensive research in the past two decades has identified not only the individual molecules of the tight junctions but also their mutual interactions, which are the focus of the present review article. While a complete map of the interactions among the tight junction molecules is probably far from being complete, the available evidence already allows outlining the general molecular architecture of the tight junctions. Here, with the aim of gaining deeper mechanistic understanding of tight junction assembly, regulation and function, we have subdivided the known molecular interactions into four major clusters that are centered on cell surface, polarity, cytoskeletal and signaling molecules.

Keywords: Abbreviations; aPKC; atypical protein kinase C; GAP; GTPase-activating protein; GST; glutathione-; S; -transferase; JAM; junctional adhesion molecule; LLGL1; lethal giant larvae-1; MAGI; membrane-associated guanylate kinase with inverted orientation; MAGUK; membrane-associated guanylate kinases; MDCK; Madin–Derby canine kidney; MUPP1; multi-PDZ domain protein-1; PI3K; phosphatidyl-inositol 3-kinase; PICK-1; protein interacting with protein C kinase-1; TGF-β; transforming growth factor-β; TJ; tight junctions; ZO; zonula occludens; ZONAB; ZO-1-associated nucleic acid bindingJunction; Adhesion; Permeability; Polarity; Cytoskeleton

Adherens and tight junctions: Structure, function and connections to the actin cytoskeleton by Andrea Hartsock; W. James Nelson (pp. 660-669).

Adherens junctions and Tight junctions comprise two modes of cell–cell adhesion that provide different functions. Both junctional complexes are proposed to associate with the actin cytoskeleton, and formation and maturation of cell–cell contacts involves reorganization of the actin cytoskeleton. Adherens junctions initiate cell–cell contacts, and mediate the maturation and maintenance of the contact. Adherens junctions consist of the transmembrane protein E-cadherin, and intracellular components, p120-catenin, β-catenin and α-catenin. Tight junctions regulate the paracellular pathway for the movement of ions and solutes in-between cells. Tight junctions consist of the transmembrane proteins occludin and claudin, and the cytoplasmic scaffolding proteins ZO-1, -2, and -3. This review discusses the binding interactions of the most studied proteins that occur within each of these two junctional complexes and possible modes of regulation of these interactions, and the different mechanisms that connect and regulate interactions with the actin cytoskeleton.

Keywords: Adherens junction; Tight junction; Actin cytoskeleton; E-cadherin; Occludin; Claudin; p120-catenin; Beta-catenin; Alpha-catenin; ZO

Structural and functional associations of apical junctions with cytoskeleton by Jun Miyoshi; Yoshimi Takai (pp. 670-691).

Actin dynamics play multiple roles in promoting cell movement, changing cell shapes, and establishing intercellular adhesion. Cell contact events are involved in tissue morphogenesis, immune responses, and cancer cell invasion. In epithelial cells, cell–cell contacts mature to form apical junctions with which the actin cytoskeleton physically associates. Living cell imaging shows, however, that the apical junctional complex is less dynamically regulated than the actin cytoskeleton, indicating that their interaction does not remain stable. Given that several cell adhesion modules are clustered at apical junctions, the sum of weak or transient interactions may create linkages that can be strong yet easily remodeled. Here we describe how subcellular protein interactions are coordinated to induce changes in actin organization and dynamics, in response to the status of apical junctions.

Keywords: Actin cytoskeleton; Cadherin; Epithelial cell polarity; Nectin; Small G protein

Biology and regulation of ectoplasmic specialization, an atypical adherens junction type, in the testis by Elissa W.P. Wong; Dolores D. Mruk; C. Yan Cheng (pp. 692-708).

Anchoring junctions are cell adhesion apparatus present in all epithelia and endothelia. They are found at the cell–cell interface (adherens junction (AJ) and desmosome) and cell–matrix interface (focal contact and hemidesmosome). In this review, we focus our discussion on AJ in particular the dynamic changes and regulation of this junction type in normal epithelia using testis as a model. There are extensive restructuring of AJ (e.g., ectoplasmic specialization, ES, a testis-specific AJ) at the Sertoli–Sertoli cell interface (basal ES) and Sertoli-elongating spermatid interface (apical ES) during the seminiferous epithelial cycle of spermatogenesis to facilitate the migration of developing germ cells across the seminiferous epithelium. Furthermore, recent findings have shown that ES also confers cell orientation and polarity in the seminiferous epithelium, illustrating that some of the functions initially ascribed to tight junctions (TJ), such as conferring cell polarity, are also part of the inherent properties of the AJ (e.g., apical ES) in the testis. The biology and regulation based on recent studies in the testis are of interest to cell biologists in the field, in particular their regulation, which perhaps is applicable to tumorigenesis.

Keywords: Anchoring junction; Adherens junction; Testis; Spermatogenesis; Ectoplasmic specialization; Atypical adherens junction

Stimulus-induced reorganization of tight junction structure: The role of membrane traffic by Dan Yu; Jerrold R. Turner (pp. 709-716).

The tight junction forms a barrier that limits paracellular movement of water, ions, and macromolecules. The permeability properties of this barrier are regulated in response to both physiological and pathophysiological stimuli, and this regulation has been modeled by pharmacological agents. Although it is now known that vesicular traffic plays important roles in tight junction assembly, the molecular mechanisms by which vesicular traffic contributes to tight junction regulation remain to be defined. This review summarizes recent progress in understanding mechanisms and pathways of tight junction protein internalization and the relevance of these to tight junction regulation.

Keywords: Tight junction; Tumor necrosis factor; Endocytosis; Cytoskeleton; Myosin; Inflammatory bowel disease

Tight junction biogenesis during early development by Judith J. Eckert; Tom P. Fleming (pp. 717-728).

The tight junction (TJ) is an essential component of the differentiated epithelial cell required for polarised transport and intercellular integrity and signalling. Whilst much can be learnt about how the TJ is constructed and maintained and how it functions using a wide range of cellular systems, the mechanisms of TJ biogenesis within developmental models must be studied to gain insight into this process as an integral part of epithelial differentiation. Here, we review TJ biogenesis in the early mammalian embryo, mainly considering the mouse but also including the human and other species, and, briefly, within the amphibian embryo. We relate TJ biogenesis to inherent mechanisms of cell differentiation and biosynthesis occurring during cleavage of the egg and the formation of the first epithelium. We also evaluate a wide range of exogenous cues, including cell–cell interactions, protein kinase C signalling, gap junctional communication, Na⁺/K⁺-ATPase and cellular energy status, that may contribute to TJ biogenesis in the embryo and how these may shape the pattern of early morphogenesis.

Keywords: Tight junction; Adherens junction; Mouse embryo; Compaction; Blastocyst; Trophectoderm; Cell polarity; Cell–cell interactions; Protein kinase C; Xenopus; embryo; Blastula

Crosstalk of tight junction components with signaling pathways by Lorenza González-Mariscal; Rocio Tapia; David Chamorro (pp. 729-756).

Tight junctions (TJs) regulate the passage of ions and molecules through the paracellular pathway in epithelial and endothelial cells. TJs are highly dynamic structures whose degree of sealing varies according to external stimuli, physiological and pathological conditions. In this review we analyze how the crosstalk of protein kinase C, protein kinase A, myosin light chain kinase, mitogen-activated protein kinases, phosphoinositide 3-kinase and Rho signaling pathways is involved in TJ regulation triggered by diverse stimuli. We also report how the phosphorylation of the main TJ components, claudins, occludin and ZO proteins, impacts epithelial and endothelial cell function.

Keywords: Abbreviations; ANP; atrial natriuretic peptide; ARPE-19; human retinal pigment epithelial cell line; AsPC-1; human pancreatic cancer cell line; BAEC; bovine aortic endothelial cells (primary culture); BBB; blood–brain barrier; BPAEC; bovine pulmonary artery endothelial cell line; BRB; blood retinal barrier; C3; transferase from; Clostridium botulinum; Caco-2; human colonic adenocarcinoma cell line; CAPAN-2; human pancreas epithelial cell line; CK2; casein kinase 2; Con8; rat mammary tumor epithelial cell line; CRIB; Cdc42 and Rac interaction binding; CRM1; chromosomal region maintenance 1; 94D; mouse cortical collecting Duct epithelial cell line; DAG; diacylglycerol; DHT; dihydrotestosterone; DiC8; phosphatidyl inositol 3,4,5-triphosphate; E; ₂; estradiol; EcN; Escherichia coli; Nissle; ECT; ₂; A guanine nucleotide exchange factor; EGF; epidermal growth factor; EGTA; ethylene glycol tetraacetic acid; EHEC; enterohemorrhagic; Escherichia coli; EMT; epithelial mesenchymal transition; EPEC; enteropathogenic; Escherichia coli; ERK; extracellular signal-regulated kinase; FAK; focal adhesion kinase; FBS; fetal bovine serum; FF; freeze–fracture; FGF; fibroblast growth factor; FHHNC; familial hypomagnesemia with hypercalciuria and nephrocalcinosis; GC; guanylate cyclase; GEF-H1; A guanine nucleotide exchange factor; GPI; glycosyl phosphatidyl inositol; GSK-3β; glycogen synthase kinase 3 beta; HBMEC; human brain microvascular endothelial cell line; HepG2; hepatic cell line; HGF; hepatocyte growth factor; HMEC; human dermal microvascular endothelial cell line; HPAEC; human pulmonary artery endothelial cell line; HT-29; human colon adenocarcinoma cell line; HUVEC; human umbilical cord endothelial cell line; ICM; inner cell mass; IEC-6; rat small intestine epithelial cell line; IFNγ; interferon gamma; IL-17; interleukine 17; JNK; c-Jun N-terminal kinase; LC; low calcium (1–5 μM Ca; ²⁺; ); Lgl; lethal giant larva; LLC-PK1; pig renal cell line; LPA; lysophosphatidic acid; MAGUK; membrane-associated guanylate kinase; MAPK; mitogen-activated protein kinase; MARCKs; myristoylated alanine-rich C kinase susbstrate; MDCK; Madin–Darby canine kidney cell line; 2ME; 2 methoxyestradiol; ML7; 1-(5-iodonaphthalene 1-sulfonyl)-1H-hexadydro-1,4-iazepine HCl; ML9; 1-(5-cloronaphthalene 1-sulfonyl)-1H-hexadydro-1,4-diazepine HCl; MLC2; regulatory myosin light chain; MYPT; myosin phosphatase target subunit; NC; normal calcium (1.8 mM Ca; ²⁺; ); NES; nuclear export signal; NLS; nuclear localization signal; NO; nitric oxide; NOS; nitric oxide synthase; N-WASP; neuronal Wiskott Aldrich syndrome protein; OmpA; outer membrane protein A; PAR-2; protease-activated receptor 2; PB1; Phox and Bem1p; PC1; Hamster pancreatic ductal carcinoma cell line; PHAII; pseudohypoaldosteronism type two; PI3K; phosphoinositide 3-kinase; PKA; protein kinase A; PKC; protein kinase C; PKG; protein kinase G; PLC γ; phospholipase C gamma; PLGF-1; placental growth factor 1; PLF; polyp-like foci; PMA; phorbol 12-myristate 13-acetate; POI; post-flight orthostatic intolerance; PP1; protein phosphatase 1; PP2A; protein phosphatase 2A; PP2B; protein phosphatase 2B; REC; retinal endothelial cells; RLE; rat lung endothelial cell line; ROMK; apical potassium channel; ROS; reactive oxygen species; SARA; Smad anchor for receptor activation protein; SGLT1; sodium glucose cotransporter; T-84; human colorectal carcinoma cell line; TAL; thick ascending limb of Henle; TEM; transmission electron microscopy; TER; transepithelial electrical resistance; TGFβ; transforming growth factor beta; TJ; tight junction; TLR2; Toll-like receptor 2; TNFα; tumor necrosis factor alpha; TPA; 12-; O; -tetradecanoyl phorbol-13-acetate; VAC; vacuolar apical compartment; VE-cadherin; endothelial cadherin; VEGF; vascular endothelial growth factor; VEGFR-2; vascular endothelial growth factor receptor; WB-F344; rat liver epithelial cell line; WNK; with no lysine kinase; Zot; zonula occludens toxinTight junction; Claudin; Occludin; ZO-1; MAPK; PI3K; AKT; Rho; MLCK; PKC; PKA; PKG

Interactions of tight junctions with membrane channels and transporters by Sigrid A. Rajasekaran; Klaus W. Beyenbach; Ayyappan K. Rajasekaran (pp. 757-769).

Tight junctions are unique organelles in epithelial cells. They are localized to the apico-lateral region and essential for the epithelial cell transport functions. The paracellular transport process that occurs via tight junctions is extensively studied and is intricately regulated by various extracellular and intracellular signals. Fine regulation of this transport pathway is crucial for normal epithelial cell functions. Among factors that control tight junction permeability are ions and their transporters. However, this area of research is still in its infancy and much more needs to be learned about how these molecules regulate tight junction structure and functions. In this review we have attempted to compile literature on ion transporters and channels involved in the regulation of tight junctions.

Keywords: Tight junction; Septate junction; Na,K-ATPase; Channel; Transporter

Tight junction and polarity interaction in the transporting epithelial phenotype by Marcelino Cereijido; Rubén G. Contreras; Liora Shoshani; David Flores-Benitez; Isabel Larre (pp. 770-793).

Development of tight junctions and cell polarity in epithelial cells requires a complex cellular machinery to execute an internal program in response to ambient cues. Tight junctions, a product of this machinery, can act as gates of the paracellular pathway, fences that keep the identity of plasma membrane domains, bridges that communicate neighboring cells. The polarization internal program and machinery are conserved in yeast, worms, flies and mammals, and in cell types as different as epithelia, neurons and lymphocytes. Polarization and tight junctions are dynamic features that change during development, in response to physiological and pharmacological challenges and in pathological situations like infection.

Keywords: Tight junction; Claudin; Zonula occludens; ZO-1; MDCK; Na,K-ATPase; PAR; Polarized transport; Epithelium; Polarity; Apical; Basolateral

Endothelial adherens and tight junctions in vascular homeostasis, inflammation and angiogenesis by Yann Wallez; Philippe Huber (pp. 794-809).

Endothelial cells lining the vessel wall are connected by adherens, tight and gap junctions. These junctional complexes are related to those found at epithelial junctions but with notable changes in terms of specific molecules and organization. Endothelial junctional proteins play important roles in tissue integrity but also in vascular permeability, leukocyte extravasation and angiogenesis. In this review, we will focus on specific mechanisms of endothelial tight and adherens junctions.

Keywords: Adherens junction; Tight junction; VE–cadherin; Claudin; Endothelium

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BBA - Biomembranes (v.1778, #3)