Chaperone-like Activity of Tubulin

Guha, S.; Manna, Tapas; Das, K. P.; Bhattacharyya, Bhabatarak

doi:10.1074/jbc.273.46.30077

Cited by 69 publications

(57 citation statements)

References 31 publications

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“…The C-terminal tail region of SNCG is rich in aspartic and glutamic acid residues, and is responsible for the flexible nature of this region. Furthermore, the tail region SNCG has a chaperone activity (34) similar to that of tubulin (35). The C-terminal tail region of SNCG was found to be placed near the GIG (146-148) motif of the BubR1.…”

Section: Molecular Modeling Of Interaction Between Sncg and Bubr1mentioning

confidence: 91%

Synuclein γ Compromises Spindle Assembly Checkpoint and Renders Resistance to Antimicrotubule Drugs

Miao

Zhang

et al. 2014

Molecular Cancer Therapeutics

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Defects in the spindle assembly checkpoint (SAC) have been proposed to contribute to the chromosomal instability in human cancers. One of the major mechanisms underlying antimicrotubule drug (AMD) resistance involves acquired inactivation of SAC. Synuclein g (SNCG), previously identified as a breast cancer-specific gene, is highly expressed in malignant cancer cells but not in normal epithelium. Here, we show that SNCG is sufficient to induce resistance to AMD-caused apoptosis in breast cancer cells and cancer xenografts. SNCG binds to spindle checkpoint kinase BubR1 and inhibits its kinase activity. Specifically, the C-terminal (Gln106-Asp127) of SNCG binds to the N-terminal TPR (tetratricopeptidelike folds) motif of BubR1. SNCG-BubR1 interaction induces a structure change of BubR1, attenuates its interaction with other key checkpoint proteins of Cdc20, and thus compromises SAC function. SNCG expression in breast cancers from patients with a neoadjuvant clinical trial showed that SNCG-positive tumors are resistant to chemotherapy-induced apoptosis. These data show that SNCG renders AMD resistance by inhibiting BubR1 activity and attenuating SAC function. Mol Cancer Ther; 13(3); 699-713. Ó2014 AACR.

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Section: Molecular Modeling Of Interaction Between Sncg and Bubr1mentioning

confidence: 91%

Synuclein γ Compromises Spindle Assembly Checkpoint and Renders Resistance to Antimicrotubule Drugs

Miao

Zhang

et al. 2014

Molecular Cancer Therapeutics

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“…In the analyses shown here, ERD10 and ERD14 demonstrated marked effects on the prevention of aggregation/deactivation of protein substrates. A comparison of related data published in the literature, such as for periplasmic disulfide isomerase of Gram-negative bacteria (DsbC; Chen et al, 1999), a-synuclein (Kim et al, 2000;Souza et al, 2000;Ahn et al, 2006), HSP90 (Minami et al, 2001), or tubulin (Guha et al, 1998), makes it safe to conclude that ERD10 and ERD14 are chaperones of commensurate potency to previously described representatives of this functional class. The significance of the effect is underlined by the fact that it far exceeds that of BSA and in several cases is commensurate with, or even exceeds, that exerted by HSP90.…”

Section: Discussionmentioning

confidence: 99%

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins

et al. 2008

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ERD10 and ERD14 (for early response to dehydration) proteins are members of the dehydrin family that accumulate in response to abiotic environmental stresses, such as high salinity, drought, and low temperature, in Arabidopsis (Arabidopsis thaliana). Whereas these proteins protect cells against the consequences of dehydration, the exact mode(s) of their action remains poorly understood. Here, detailed evidence is provided that ERD10 and ERD14 belong to the family of intrinsically disordered proteins, and it is shown in various assays that they act as chaperones in vitro. ERD10 and ERD14 are able to prevent the heat-induced aggregation and/or inactivation of various substrates, such as lysozyme, alcohol dehydrogenase, firefly luciferase, and citrate synthase. It is also demonstrated that ERD10 and ERD14 bind to acidic phospholipid vesicles without significantly affecting membrane fluidity. Membrane binding is strongly influenced by ionic strength. Our results show that these intrinsically disordered proteins have chaperone activity of rather wide substrate specificity and that they interact with phospholipid vesicles through electrostatic forces. We suggest that these findings provide the rationale for the mechanism of how these proteins avert the adverse effects of dehydration stresses.

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“…For nonthermal aggregation of substrate proteins, insulin became a popular choice for as the assay system, because reduction of disulfide bond by DTT leads to aggregation of its B-chain at room temperature (16,26,40). Like other chaperones, ␣ s -casein also can prevent disulfide cleavage-induced aggregation of insulin at 27°C, requiring a 1:0.35 weight ratio between insulin and ␣ s -casein for complete prevention of aggregation (Fig.…”

Section: Fig 2 Prevention Of Thermal Aggregation Of Whey Proteins Bmentioning

confidence: 99%

“…TriC has a ring-like structure of 8 to 9 subunits (10). Tubulin, reported recently by us (16) to act like a chaperone, associates to form microtubules. ␣-Crystallin, which belongs to small heat shock protein (sHSP) family (17), has been proposed to have a micellar architecture (11,12).…”

mentioning

confidence: 99%

Molecular Chaperone-like Properties of an Unfolded Protein, αs-Casein

Bhattacharyya¹,

Das

1999

Journal of Biological Chemistry

181

159

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All molecular chaperones known to date are well organized, folded protein molecules whose three-dimensional structure are believed to play a key role in the mechanism of substrate recognition and subsequent assistance to folding. A common feature of all protein and nonprotein molecular chaperones is the propensity to form aggregates very similar to the micellar aggregates. In this paper we show that ␣ s -casein, abundant in mammalian milk, which has no well defined secondary and tertiary structure but exits in nature as a micellar aggregate, can prevent a variety of unrelated proteins/ enzymes against thermal-, chemical-, or light-induced aggregation. It also prevents aggregation of its natural substrates, the whey proteins. ␣ s -Casein interacts with partially unfolded proteins through its solvent-exposed hydrophobic surfaces. The absence of disulfide bridge or free thiol groups in its sequence plays important role in preventing thermal aggregation of whey proteins caused by thiol-disulfide interchange reactions. Our results indicate that ␣ s -casein not only prevents the formation of huge insoluble aggregates but it can also inhibit accumulation of soluble aggregates of appreciable size. Unlike other molecular chaperones, this protein can solubilize hydrophobically aggregated proteins. This protein seems to have some characteristics of cold shock protein, and its chaperone-like activity increases with decrease of temperature.

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Chaperone-like Activity of Tubulin

Cited by 69 publications

References 31 publications

Synuclein γ Compromises Spindle Assembly Checkpoint and Renders Resistance to Antimicrotubule Drugs

Synuclein γ Compromises Spindle Assembly Checkpoint and Renders Resistance to Antimicrotubule Drugs

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins

Molecular Chaperone-like Properties of an Unfolded Protein, αs-Casein

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