Association of clathrin, AP-2 adaptor and actin cytoskeleton with developing interlocking membrane domains of lens fibre cells

Zhou, Chengjing; Lo, Woo-Kuen

doi:10.1016/s0014-4835(03)00171-4

Cited by 32 publications

(42 citation statements)

References 41 publications

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“…Lens fiber cells have an extensive cortical actin cytoskeleton that is reinforced by actin bundles that are found at vertices of the hexagonal fiber cell (Lo et al, 1997b). Further, membrane protrusions, which increase the membrane surface area between fiber cells, and help to minimize light scatter (Bassnett et al, 2011), are stabilized by an F-actin network within each protrusion (Zhou and Lo, 2003). Thus, the disruption of the normal hexagonal geometry of lens fiber cells (Figure 7 and supplemental figures 3–5) and the loss of membrane protrusions (Figure 3) seen in cKO lens fiber cells is likely directly due to the destabilization of the F-actin cytoskeleton.…”

Section: Discussionmentioning

confidence: 99%

Beta-1 integrin is important for the structural maintenance and homeostasis of differentiating fiber cells

Scheiblin

Gao

Caplan

et al. 2014

The International Journal of Biochemistry & Cell Biology

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β1-integrin is a heterodimeric transmembrane protein that has roles in both cell-extracellular matrix and cell-cell interactions. Conditional deletion of β1-integrin from all lens cells during embryonic development results in profound lens defects, however, it is less clear whether this reflects functions in the lens epithelium alone or whether this protein plays a role in lens fibers. Thus, a conditional approach was used to delete β1-integrin solely from the lens fiber cells. This deletion resulted in two distinct phenotypes with some lenses exhibiting cataracts while others were clear, albeit with refractive defects. Analysis of “clear” conditional knockout lenses revealed that they had profound defects in fiber cell morphology associated with the loss of the F-actin network. Physiological measurements found that the lens fiber cells had a two-fold increase in gap junctional coupling, perhaps due to differential localization of connexins 46 and 50, as well as increased water permeability. This would presumably facilitate transport of ions and nutrients through the lens, and may partially explain how lenses with profound structural abnormalities can maintain transparency. In summary, β1-integrin plays a role in maintaining the cellular morphology and homeostasis of the lens fiber cells.

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Section: Discussionmentioning

confidence: 99%

Beta-1 integrin is important for the structural maintenance and homeostasis of differentiating fiber cells

Scheiblin

Gao

Caplan

et al. 2014

The International Journal of Biochemistry & Cell Biology

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“…The integrity of fiber cells depends on the normal and extensive distributions of its unique interlocking system (Cohen, 1965; Dickson and Crock, 1972; Kuwabara, 1975; Kuszak et al, 1980; Willekens and Vrensen, 1982; Kistler et al, 1986; Zhou and Lo, 2003; Lo et al, 2014) and adherens junctions (Volk and Geiger, 1986; Geiger et al, 1987; Lo, 1988; Atreya et al, 1989; Maisel and Atreya, 1990; Lo et al, 2000; Bagchi et al, 2002; Straub et al, 2003) within the lens. It has been previously suggested that the interlocking protrusions may assist in an overall stability of fiber-cells at the gross level, while adherens junctions maintain localized adhesions in protrusions and between fiber cells at the microscopic level (Lo, 1988; Lo and Reese, 1993; Zhou and Lo, 2003).…”

Section: Introductionmentioning

confidence: 99%

“…It has been previously suggested that the interlocking protrusions may assist in an overall stability of fiber-cells at the gross level, while adherens junctions maintain localized adhesions in protrusions and between fiber cells at the microscopic level (Lo, 1988; Lo and Reese, 1993; Zhou and Lo, 2003). …”

Section: Introductionmentioning

confidence: 99%

Breakdown of interlocking domains may contribute to formation of membranous globules and lens opacity in ephrin-A5−/− mice

Biswas

Son

et al. 2016

Experimental Eye Research

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Ephrin-A5, a ligand of the Eph family of receptor tyrosine kinases, plays a key role in lens fiber cell packing and cell-cell adhesion, with approximately 87% of ephrin-A5−/− mice develop nuclear cataracts. Here, we investigated the extensive formation of light-scattering globules associated with breakdown of interlocking protrusions during lens opacification in ephrin-A5−/− mice. Lenses from wild-type (WT) and ephrin-A5−/− mice between 2–21 weeks old were studied with light and electron microscopy, immunofluorescence labeling, freeze-fracture TEM and filipin cytochemistry for membrane cholesterol detection. Lens opacities with various densities were first observed in ephrin-A5−/− mice at around 60 days old. Dense cataracts in the mutant lenses were seen primarily in the nuclear region surrounded by transparent cortices from all eyes examined. We confirmed that a majority of nuclear cataracts were dislocated posteriorly and ruptured the thinner posterior lens capsule. SEM analysis indicated that numerous interlocking protrusions and wavy ridge-and-valley membrane surfaces in deep cortical and nuclear fibers did not cause lens opacity in both transparent ephrin-A5−/− and WT mice. In contrast, abundant isolated membranous globules of approximately 1,000 nm in size were distributed randomly along the intact fiber cells during early stage of all ephrin-A5−/− cataracts examined. A further examination using both SEM and TEM revealed that isolated globules were generated from the disintegrated interlocking protrusions originally located along the corners of hexagonal fiber cells. Freeze-fracture TEM further revealed the association of square-array aquaporin junctions with both isolated globules and interlocking membrane domains. This study reports for the first time that disrupted interlocking protrusions are the source of numerous large membranous globules that contribute to light scattering and nuclear cataracts in the ephrin-A5−/− mice. Our results further suggest that dissociations of N-cadherin and adherens junctions in the associated interlocking domains may result in the formation of isolated globules and nuclear opacities in the ephrin-A5−/− mice.

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“…During lens fiber cell differentiation, these cells develop elaborated lateral membranes that form high surface area interdigitations with their neighbors to allow for extensive cell communication in this avascular tissue (51). Because these interdigitations also are tightly associated with the actin cytoskeleton (52), this association supports a Bin3 connection in actin cytoskeletal dynamics and membrane structure. However, if this is the case, it remains unclear why the lens phenotype should develop so late, only after eye lid opening.…”

Section: Discussionmentioning

confidence: 91%

Bin3 Deletion Causes Cataracts and Increased Susceptibility to Lymphoma during Aging

et al. 2008

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Association of clathrin, AP-2 adaptor and actin cytoskeleton with developing interlocking membrane domains of lens fibre cells

Cited by 32 publications

References 41 publications

Beta-1 integrin is important for the structural maintenance and homeostasis of differentiating fiber cells

Beta-1 integrin is important for the structural maintenance and homeostasis of differentiating fiber cells

Breakdown of interlocking domains may contribute to formation of membranous globules and lens opacity in ephrin-A5−/− mice

Bin3 Deletion Causes Cataracts and Increased Susceptibility to Lymphoma during Aging

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