The calcium-binding site of clathrin light chains.

Näthke, Inke; Hill, Bl L.; Parham, Peter; Brodsky, FM

doi:10.1016/s0021-9258(17)44797-1

Cited by 38 publications

(8 citation statements)

References 46 publications

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“…Clathrin is a protein involved in the formation of coated vesicles, which is also required for the stabilization of fibres of the mitotic spindle . In particular, CLTA which is a calcium-binding protein, plays a key role in reinforcing the stability of clathrin heavy chain trimers which in turn provide the structural backbone of the clathrin lattice. Interestingly, it has been demonstrated that monomeric, but not trimeric, clathrin heavy chain functions as a coactivator for p53 and regulates p53-mediated transcription. , Here, we reported that CLTA is down-regulated (2.7-fold) in IGROV-1 cells treated by ST3595.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Cellular Response to Novel Proapoptotic Agents Related to Atypical Retinoids in Human IGROV-1 Ovarian Carcinoma Cells

et al. 2010

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Novel agents characterized by the scaffold of the atypical retinoid ST1926, but containing different chemical functions (carboxylic or hydroxamic acid), exhibit potent proapoptotic activity. In the present paper, we show that the treatment of the IGROV-1 ovarian cancer cell line with compounds sharing structural features with ST1926 (ST1898, ST3595, ST3056) determines a strong inhibition of proliferation mainly due to apoptotic cell death. In an effort to understand the mechanism of action of these compounds, we performed a proteomics analysis of IGROV-1 total lysates and nuclear extracts. Using this approach, we found that deregulation of calcium homeostasis, oxidative stress, cytoskeleton reorganization, and deregulation of proteasome function may represent important pathways involved in response of IGROV-1 cells to the studied compounds. The most prominent effect was down-regulation of factors involved in protein degradation, an event more marked in cells treated with ST3595. In addition, we identified proteins specifically modulated by each treatment, including prohibitin and cochaperone P23 (ST1898), pre-mRNA splicing factor SF2p32 and clathrin light chain (ST3595), as well as Far upstream element (FUSE) binding protein 1 and DNA-binding protein B (ST3056). By identifying proteins modulated by novel proapoptotic agents, this study provides insights into critical aspects of their mechanism of action.

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Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Cellular Response to Novel Proapoptotic Agents Related to Atypical Retinoids in Human IGROV-1 Ovarian Carcinoma Cells

et al. 2010

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“…Determining the number of low-affinity sites is obscured by spectrin aggregation which occurs long before the sites are titrated to end point in vitro. Because low-affinity divalent cation sites have been described which contain only a single acidic residue (Nathke et al, 1990), spectrin may contain almost as many low-affinity sites as there are acidic amino acids. The secondary and higher order structures of spectrin are arranged to maximally expose its large number of acidic amino acids (Parry & Cohen, 1991).…”

Section: Discussionmentioning

confidence: 99%

Divalent cation binding to erythrocyte spectrin

Wallis¹,

Babitch²,

Wenegieme³

1993

Biochemistry

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Erythrocyte spectrin dimers and separated alpha- and beta-spectrin chains bound 45Ca2+ after electrophoresis on native or sodium dodecyl sulfate-polyacrylamide gels, blotting, and 45Ca2+ overlay. Flow dialysis and equilibrium dialysis revealed two binding components: high-affinity, Ca(2+)-specific sites with kd = 4 x 10(-7) M and n = 100 +/- 20 per dimer and a low-affinity (millimolar) divalent cation component. Whereas brain spectrin had only four high-affinity sites [Wallis, C. J., Wenegieme, E. F., & Babitch, J. A. (1992) J. Biol. Chem. 267, 4333-4337], erythrocyte spectrin had 25-fold more sites per dimer. In addition to possibly modifying spectrin interactions with calcium-dependent protease and actin, as suggested by previous work on the interaction of Ca2+ with brain spectrin, the approximately two high-affinity sites per repeating segment of erythrocyte spectrin appear to stabilize a folded conformation of repeat structures indicated by an entropy increase upon binding. These data support the hypothesis that divalent cation binding to erythrocyte spectrin has become specialized to stabilize the membrane skeletal network and the cell, making them flexible but resistant to shear under the stressful conditions of blood circulation.

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“…CLCa has an Hsc70 binding sequence that was shown to stimulate uncoating in vitro ( DeLuca-Flaherty et al, 1990 ). However later studies suggested that uncoating of vesicles could also be done in the absence of CLCs in vitro ( Ungewickell et al, 1995 ) Both the light chains also have a calcium binding region ( Nathke et al, 1990 ) and calmodulin binding domain ( Pley et al, 1995 ) present at the centre and C-terminal, respectively. While these domains have been found to play a role in in vitro studies, no function has been attributed to them in vivo .…”

Section: Clathrin Light Chain Domain Organization and Functionmentioning

confidence: 99%

Clathrin Light Chains: Not to Be Taken so Lightly

Das

Tiwari

Subramanyam

2021

Front. Cell Dev. Biol.

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Clathrin is a cytosolic protein involved in the intracellular trafficking of a wide range of cargo. It is composed of three heavy chains and three light chains that together form a triskelion, the subunit that polymerizes to form a clathrin coated vesicle. In addition to its role in membrane trafficking, clathrin is also involved in various cellular and biological processes such as chromosomal segregation during mitosis and organelle biogenesis. Although the role of the heavy chains in regulating important physiological processes has been well documented, we still lack a complete understanding of how clathrin light chains regulate membrane traffic and cell signaling. This review highlights the importance and contributions of clathrin light chains in regulating clathrin assembly, vesicle formation, endocytosis of selective receptors and physiological and developmental processes.

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The calcium-binding site of clathrin light chains.

Cited by 38 publications

References 46 publications

Proteomic Analysis of Cellular Response to Novel Proapoptotic Agents Related to Atypical Retinoids in Human IGROV-1 Ovarian Carcinoma Cells

Proteomic Analysis of Cellular Response to Novel Proapoptotic Agents Related to Atypical Retinoids in Human IGROV-1 Ovarian Carcinoma Cells

Divalent cation binding to erythrocyte spectrin

Clathrin Light Chains: Not to Be Taken so Lightly

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