Biophysical characterization of the isolated C‐terminal region of the transient receptor potential vanilloid 1

Aguado-Llera, David; Bacarizo, Julio; Gregorio-Teruel, Lucía; Taberner, Francisco J.; Cámara-Artigas, A.; Neira, José L.

doi:10.1016/j.febslet.2012.03.030

Cited by 5 publications

(3 citation statements)

References 51 publications

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“…hCOA3 is one of the few characterized, unstructured, flexible proteins that self-associates in solution, ,,, showing several oligomeric species [as judged from the hydrodynamic experiments (Figure )]. We hypothesize that this self-association could have several functions.…”

Section: Discussionmentioning

confidence: 99%

Human COA3 Is an Oligomeric Highly Flexible Protein in Solution

et al. 2016

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The assembly of the protein complex of cytochrome c oxidase (COX), which participates in the mitochondrial respiratory chain, requires a large number of accessory proteins (the so-called assembly factors). Human COX assembly factor 3 (hCOA3), also known as MITRAC12 or coiled-coil domain-containing protein 56 (CCDC56), interacts with the first subunit protein of COX to form its catalytic core and promotes its assemblage with the other units. Therefore, hCOA3 is involved in COX biogenesis in humans and can be exploited as a drug target in patients with mitochondrial dysfunctions. However, to be considered a molecular target, its structure and conformational stability must first be elucidated. We have embarked on the description of such features by using spectroscopic and hydrodynamic techniques, in aqueous solution and in the presence of detergents, together with computational methods. Our results show that hCOA3 is an oligomeric protein, forming aggregates of different molecular masses in aqueous solution. Moreover, on the basis of fluorescence and circular dichroism results, the protein has (i) its unique tryptophan partially shielded from solvent and (ii) a relatively high percentage of secondary structure. However, this structure is highly flexible and does not involve hydrogen bonding. Experiments in the presence of detergents suggest a slightly higher content of nonrigid helical structure. Theoretical results, based on studies of the primary structure of the protein, further support the idea that hCOA3 is a disordered protein. We suggest that the flexibility of hCOA3 is crucial for its interaction with other proteins to favor mitochondrial protein translocation and assembly of proteins involved in the respiratory chain.

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Section: Discussionmentioning

confidence: 99%

Human COA3 Is an Oligomeric Highly Flexible Protein in Solution

et al. 2016

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“…In this regard, it is important to mention that an in‐depth biophysical characterization indicates that the C‐terminal cytoplasmic domain of TRPV1 is mostly unstructured (Aguado‐Llera et al . ). Therefore, tubulin interaction can provide stability to certain region, especially the interacting region.…”

Section: Evolutionary Significance Of Trpv1–tubulin Interactionmentioning

confidence: 97%

TRPV1–tubulin complex: involvement of membrane tubulin in the regulation of chemotherapy‐induced peripheral neuropathy

Goswami

2012

Journal of Neurochemistry

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Existence of microtubule cytoskeleton at the membrane and submembranous regions, referred as ‘membrane tubulin’ has remained controversial for a long time. Since we reported physical and functional interaction of Transient Receptor Potential Vanilloid Sub Type 1 (TRPV1) with microtubules and linked the importance of TRPV1‐tubulin complex in the context of chemotherapy‐induced peripheral neuropathy, a few more reports have characterized this interaction in in vitro and in in vivo condition. However, the cross‐talk between TRPs with microtubule cytoskeleton, and the complex feedback regulations are not well understood. Sequence analysis suggests that other than TRPV1, few TRPs can potentially interact with microtubules. The microtubule interaction with TRPs has evolutionary origin and has a functional significance. Biochemical evidence, Fluorescence Resonance Energy Transfer analysis along with correlation spectroscopy and fluorescence anisotropy measurements have confirmed that TRPV1 interacts with microtubules in live cell and this interaction has regulatory roles. Apart from the transport of TRPs and maintaining the cellular structure, microtubules regulate signaling and functionality of TRPs at the single channel level. Thus, TRPV1‐tubulin interaction sets a stage where concept and parameters of ‘membrane tubulin’ can be tested in more details. In this review, I critically analyze the advancements made in biochemical, pharmacological, behavioral as well as cell‐biological observations and summarize the limitations that need to be overcome in the future.

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“…Since then, other examples of homo-and heterodimeric complexes of IDPs/IDRs with their disordered or wellfolded protein partners where IDP/IDR remain largely disordered upon binding have been reported and reviewed in detail elsewhere [5][6][7][8][9][10]. Table 1 summarizes some of the advancements in this field, focusing on IDP/IDP (IDR/IDR) homo-and heterodimers [2,4,[11][12][13][14][15][16][17][18].…”

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Letter to the Editor: No folding upon binding of intrinsically disordered proteins: Still interesting but not unique and novel. A commentary on “A novel mode of interaction between intrinsically disordered proteins. by Hibino, E. and Hoshino, M., Biophysics and Physicobiology 17, 86–93 (2020). DOI: 10.2142/biophysico.BSJ-2020012”

Sigalov

2020

BIOPHYSICS

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The emergence of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) has introduced a new paradigm of coupled binding and folding that suggests that IDPs and IDRs fold upon binding to their partners [1]. However, in 2004, a novel and previously unrecognized no folding upon binding mechanism has been first reported for several IDPs-cytoplasmic domains of signaling subunits from different cell receptors: ζ cyt , CD3δ cyt , CD3ε cyt , CD3γ cyt , FcRγ cyt , Igα cyt and Igβ cyt [2]. The IDPs studied in this work were all found to form specific homodimers under physiological conditions without folding upon dimerization [2]. This unusual phenomenon is distinct from non-specific aggregation behavior seen in many systems (e.g., elastin [3]). Later, in 2007, the no folding upon binding mechanism has been demonstrated for the heterodimeric complex of the well-folded simian immunodeficiency virus (SIV) Nef protein and intrinsically disordered ζ cyt where ζ cyt

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Biophysical characterization of the isolated C‐terminal region of the transient receptor potential vanilloid 1

Cited by 5 publications

References 51 publications

Human COA3 Is an Oligomeric Highly Flexible Protein in Solution

Human COA3 Is an Oligomeric Highly Flexible Protein in Solution

TRPV1–tubulin complex: involvement of membrane tubulin in the regulation of chemotherapy‐induced peripheral neuropathy

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