Claudin-10 exists in six alternatively spliced isoforms that exhibit distinct localization and function

Günzel, Dorothee; Stuiver, Marchel; Kausalya, P. Jaya; Haisch, Lea; Krug, Susanne M.; Rosenthal, Rita; Meij, Iwan C.; Hunziker, Walter; Fromm, Michael; Müller, Dominik

doi:10.1242/jcs.040113

Cited by 171 publications

(211 citation statements)

References 29 publications

(45 reference statements)

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“…In the present study, mice lacking claudin-10 in the TAL presented with disturbances in the homeostasis of Ca 2+ and Mg 2+ homeostasis, as evidenced by hypocalcemia, hypermagnesemia, hyperphosphatemia, and nephrocalcinosis. Based on our data and that of others, the claudin-10 isoform expressed in this nephron segment is claudin-10b (9,17,18). Accordingly, using the ksp-cre mouse line, we specifically ablated claudin-10b expression in the TAL, but did not alter expression of claudin-10a in the PCT, as demonstrated by immunohistology and qPCR (Fig.…”

Section: Discussionsupporting

confidence: 67%

“…This TJ protein is expressed in two isoforms, claudin-10a and claudin-10b, which differ in their first extracellular loop (9,17). In cultured epithelial cells, heterologous expression of claudin-10a increases paracellular anion transport, whereas claudin-10b expression increases paracellular cation transport.…”

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confidence: 99%

“…In cultured epithelial cells, heterologous expression of claudin-10a increases paracellular anion transport, whereas claudin-10b expression increases paracellular cation transport. Both isoforms are expressed differentially along the nephron, with claudin-10a found predominantly in cortical segments, whereas claudin-10b is enriched in the medullary region (9,17,18).…”

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confidence: 99%

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Deletion of claudin-10 ( Cldn10 ) in the thick ascending limb impairs paracellular sodium permeability and leads to hypermagnesemia and nephrocalcinosis

Breiderhoff

Himmerkus

Stuiver

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Section: Discussionsupporting

confidence: 67%

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confidence: 99%

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Deletion of claudin-10 ( Cldn10 ) in the thick ascending limb impairs paracellular sodium permeability and leads to hypermagnesemia and nephrocalcinosis

Breiderhoff

Himmerkus

Stuiver

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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145

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“…claudin-2, 10b, 15), anion-selectivity (e.g. claudin-10a, 17), or preferentially sealing claudins (e.g., claudin-1) 73,[78][79][80][81][82][83][84][85] . The latter group are claudins that have not (yet) been associated with promoting permeability of a specific type of ion or molecule, and are hence thought to enhance the barrier function.…”

Section: Regulation Of Paracellular Permeabilitymentioning

confidence: 99%

Tight junctions: from simple barriers to multifunctional molecular gates

Zihni

Mills

Matter

et al. 2016

Nat Rev Mol Cell Biol

1,025

877

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Main body of text: 5983 words 2Epithelia and endothelia separate different tissue compartments and protect multicellular organisms form the outside world. This requires the formation of tight junctions, selective gates that control paracellular diffusion of ions and solutes. Tight junctions also form the border between the apical and basolateral plasma membrane domains and are linked to the machinery that controls apicobasal polarization. Additionally, signalling networks that guide diverse cell behaviours and functions are connected to tight junctions, transmitting information to and from the cytoskeleton, nucleus and different cell adhesion complexes. Here, we discuss recent advances in our understanding of the molecular architecture and cellular functions of tight junctions.Microscopists in the 19 th century described the paracellular space between neighbouring cells within an epithelial sheet to be sealed by a "terminal bar", a structure later resolved by electron microscopy into a composite of distinct cell-cell junctions that is now called the epithelial junctional complex and is formed by tight junctions, adherens junctions and desmosomes 1,2 . As the former two junctions are more tightly associated and often reside at the apical end of the lateral membrane, they are often referred to as the apical junctional complex (however, in endothelia, tight junctions and adherens junctions can be intercalated) (Fig. 1). Tight junctions are essential for barrier formation, and their primary physiological role is to function as paracellular gates that restrict diffusion on the basis of size and charge. Selective paracellular diffusion is an essential process for the maintenance of homoeostasis in organs and tissues. Tight junctions have long been the most enigmatic of all adhesion complexes and eluded a detailed molecular and functional analysis due to their complex architecture. Recent years have witnessed the identification of a large array of components associated with tight junctions implicating these junctions in an unexpected range of different functions, thereby challenging the traditional model, in which tight junctions are considered a simple diffusion barrier formed by a rigid molecular complex. In line with these various functions, mutations in genes encoding tight junction proteins have been linked to a range of inherited human diseases. Additionally, tight junction components are known to be targeted by a number of pathogenic bacteria and viruses, which hijack tight junction proteins to enter and infect cells, or target junctional signalling mechanisms to cross tissue barriers. Although tight junctions are a vertebrate junction, many of their components and functions are evolutionarily conserved (Box 1).The main purpose of this review is to examine the recent advances in the unravelling of the molecular architecture of tight junctions and understanding their functions. We will discuss recent exciting insights into how tight junctions function as signalling platforms that guide cell behaviour and differen...

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“…Single-ion permeabilities were determined from dilution or bi-ionic potentials and the Goldman-Hodgkin-Katz equation as reported previously (Amasheh et al, 2002;Gü nzel et al, 2009;Yu et al;. Briefly, NaCl dilution potentials were measured by switching one hemichamber to a solution containing a reduced concentration of NaCl and all other components identical to standard Ringer's.…”

Section: Electrophysiologymentioning

confidence: 99%

Tricellulin Forms a Barrier to Macromolecules in Tricellular Tight Junctions without Affecting Ion Permeability

Krug

Amasheh

Richter

et al. 2009

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Tricellulin is a tight junction protein localized in tricellular tight junctions (tTJs), the meeting points of three cells, but also in bicellular tight junctions (bTJs). To investigate its specific barrier functions in bTJs and tTJs, TRIC-a was expressed in low-level tricellulin-expressing cells, and MDCK II, either in all TJs or only in tTJs. When expressed in all TJs, tricellulin increased paracellular electrical resistance and decreased permeability to ions and larger solutes, which are associated with enhanced ultrastructural integrity of bTJs toward enhanced strand linearity. In tTJs in contrast, ultrastructure was unchanged and tricellulin minimized permeability to macromolecules but not to ions. This paradox is explained by properties of the tTJ central tube which is wide enough for passage of macromolecules, but too rare to contribute significantly to ion permeability. In conclusion, at low tricellulin expression the tTJ central tube forms a pathway for macromolecules. At higher expression, tricellulin forms a barrier in tTJs effective only for macromolecules and in bTJs for solutes of all sizes.

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Claudin-10 exists in six alternatively spliced isoforms that exhibit distinct localization and function

Cited by 171 publications

References 29 publications

Deletion of claudin-10 ( Cldn10 ) in the thick ascending limb impairs paracellular sodium permeability and leads to hypermagnesemia and nephrocalcinosis

Deletion of claudin-10 ( Cldn10 ) in the thick ascending limb impairs paracellular sodium permeability and leads to hypermagnesemia and nephrocalcinosis

Tight junctions: from simple barriers to multifunctional molecular gates

Tricellulin Forms a Barrier to Macromolecules in Tricellular Tight Junctions without Affecting Ion Permeability

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