Mapping Functional Domains of Chloride Intracellular Channel (CLIC) Proteins in Vivo

Berry, Katherine L.; Hobert, Oliver

doi:10.1016/j.jmb.2006.04.046

Cited by 45 publications

(82 citation statements)

References 56 publications

(93 reference statements)

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“…Each of the two CLICs encoded by C. elegans is able to support tubulogenesis and only cell-specific expression prevents functional complementation in vivo. 6,32 In mammals, CLIC1 is widely expressed in virtually all tissues and cell types and is present in primary cultures of mouse endothelial cells (not shown). Our hypothesis is that functional redundancy between CLIC4 and other CLICs is adequate to allow a fraction of Clic4 Ϫ/Ϫ mice to survive through embryogenesis to birth and to allow essentially normal postnatal growth and development in the unstressed laboratory environment.…”

Section: Discussionmentioning

confidence: 99%

Chloride Intracellular Channel Protein-4 Functions in Angiogenesis by Supporting Acidification of Vacuoles Along the Intracellular Tubulogenic Pathway

Ulmasov

Bruno

Gordon

et al. 2009

The American Journal of Pathology

118

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Endothelial cells form capillary tubes through the process of intracellular tubulogenesis. Chloride intracellular channel (CLIC) family proteins have been previously implicated in intracellular tubulogenesis, but their specific role has not been defined. In this study, we show that disruption of the Clic4 gene in mice results in defective angiogenesis in vivo as reflected in a Matrigel plug angiogenesis assay. An angiogenesis defect is also apparent in the retina, both in the decreased spontaneous development of retinal vasculature of unstressed mice and in the dramatically decreased angiogenic response of retinal vessels to an oxygen toxicity challenge. We found that endothelial cells derived from Clic4 ؊/؊ mice demonstrated impaired tubulogenesis in three-dimensional fibrin gels compared with cells derived from wild-type mice. Furthermore, we found that tubulogenesis of wildtype cells in culture was inhibited by both an inhibitor of CLICs and an inhibitor of the vacuolar proton ATPase. Finally, we showed that vacuoles along the endothelial tubulogenesis pathway are acidic in wildtype cells, and that vacuolar acidification is impaired in Clic4 ؊/؊ cells while lysosomal acidification is intact. We conclude that CLIC4 plays a critical role in angiogenesis by supporting acidification of vacuoles along the cell-hollowing tubulogenic pathway.

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Section: Discussionmentioning

confidence: 99%

Chloride Intracellular Channel Protein-4 Functions in Angiogenesis by Supporting Acidification of Vacuoles Along the Intracellular Tubulogenic Pathway

Ulmasov

Bruno

Gordon

et al. 2009

The American Journal of Pathology

118

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“…CLICs are putative ion channels belonging to the p64 gene family and are distantly related to GSTs. They exist as both soluble cytoplasmic proteins and membrane bound channel proteins with a putative transmembrane domain near the amino terminus, making them unique as mammalian ion channels (Redhead et al 1997;Berry and Hobert 2006). Of the six known mammalian CLICs, only CLIC1 and CLIC4 are expressed highly in endothelial cells Money et al 2007;Suh et al 2007;Ulmasov et al 2007;Tung et al 2009;Tung and Kitajewski 2010;Wegner et al 2010).…”

Section: Jj Tung Et Almentioning

confidence: 99%

Tips, Stalks, Tubes: Notch-Mediated Cell Fate Determination and Mechanisms of Tubulogenesis during Angiogenesis

Tung¹,

Tattersall²,

Kitajewski³

2011

Cold Spring Harbor Perspectives in Medicine

104

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“…In Caenorhabditis elegans, disruption of the CLIC homolog EXC-4 dramatically impairs formation and maintenance of the intracellular excretory tube, but vertebrate CLICs cannot rescue the phenotype, indicating that vertebrate and invertebrate CLICs have distinct functions (Berry et al, 2003;Berry and Hobert, 2006).…”

Section: Introductionmentioning

confidence: 99%

CLIC4 regulates cell adhesion and β1 integrin trafficking

Argenzio

Margadant

Leyton-Puig

et al. 2014

Journal of Cell Science

100

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BSTRACTChloride intracellular channel protein 4 (CLIC4) exists in both soluble and membrane-associated forms, and is implicated in diverse cellular processes, ranging from ion channel formation to intracellular membrane remodeling. CLIC4 is rapidly recruited to the plasma membrane by lysophosphatidic acid (LPA) and serum, suggesting a possible role for CLIC4 in exocytic-endocytic trafficking. However, the function and subcellular target(s) of CLIC4 remain elusive. Here, we show that in HeLa and MDA-MB-231 cells, CLIC4 knockdown decreases cell-matrix adhesion, cell spreading and integrin signaling, whereas it increases cell motility. LPA stimulates the recruitment of CLIC4 to b1 integrin at the plasma membrane and in Rab35-positive endosomes. CLIC4 is required for both the internalization and the serum-or LPA-induced recycling of b1 integrin, but not for EGF receptor trafficking. Furthermore, we show that CLIC4 suppresses Rab35 activity and antagonizes Rab35-dependent regulation of b1 integrin trafficking. Our results define CLIC4 as a regulator of Rab35 activity and serum-and LPAdependent integrin trafficking.

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Mapping Functional Domains of Chloride Intracellular Channel (CLIC) Proteins in Vivo

Cited by 45 publications

References 56 publications

Chloride Intracellular Channel Protein-4 Functions in Angiogenesis by Supporting Acidification of Vacuoles Along the Intracellular Tubulogenic Pathway

Chloride Intracellular Channel Protein-4 Functions in Angiogenesis by Supporting Acidification of Vacuoles Along the Intracellular Tubulogenic Pathway

Tips, Stalks, Tubes: Notch-Mediated Cell Fate Determination and Mechanisms of Tubulogenesis during Angiogenesis

CLIC4 regulates cell adhesion and β1 integrin trafficking

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