Structural basis of the signal transduction via transmembrane domain of the human growth hormone receptor

Bocharov, Eduard V.; Lesovoy, Dmitry M.; Bocharova, Olga V.; Urban, Anatoly S.; Павлов, Константин; Volynsky, Pavel E.; Efremov, Roman G.; Arseniev, Alexander S.

doi:10.1016/j.bbagen.2018.03.022

Cited by 31 publications

(33 citation statements)

References 51 publications

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“…When investigating a specific protein target, a 5-20% cis ratio was observed by NMR (average: 10%) [38]. Moreover, it is known that the type of the proceeding amino acid strongly influences the cistrans ratio: aromatic residues increase the presence of the cis isomer (e.g., Trp-Pro 37.7%; Phe-Pro 23% [39] or 29% [40]). In summary, it appears that, depending on the amino acid proceeding the proline [39], the cis portion is around 5-30% (25% in average) in folded proteins.…”

Section: Fkbp-type Immunophilinsmentioning

confidence: 99%

A twist in the ABC: regulation of ABC transporter trafficking and transport by FK506‐binding proteins

Geisler

Hegedüs

2020

FEBS Letters

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Post‐transcriptional regulation of ATP‐binding cassette (ABC) proteins has been so far shown to encompass protein phosphorylation, maturation, and ubiquitination. Yet, recent accumulating evidence implicates FK506‐binding proteins (FKBPs), a type of peptidylprolyl cis–trans isomerase (PPIase) proteins, in ABC transporter regulation. In this perspective article, we summarize current knowledge on ABC transporter regulation by FKBPs, which seems to be conserved over kingdoms and ABC subfamilies. We uncover striking functional similarities but also differences between regulatory FKBP‐ABC modules in plants and mammals. We dissect a PPIase‐ and HSP90‐dependent and independent impact of FKBPs on ABC biogenesis and transport activity. We propose and discuss a putative new mode of transient ABC transporter regulation by cis–trans isomerization of X‐prolyl bonds.

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Section: Fkbp-type Immunophilinsmentioning

confidence: 99%

A twist in the ABC: regulation of ABC transporter trafficking and transport by FK506‐binding proteins

Geisler

Hegedüs

2020

FEBS Letters

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“…The second model proposes that the conformational change in the transmembrane domain causes rearrangements in the lipids of the inner plasma membrane, which drive the changes in the intracellular regions and bound JAK2 proteins. Due to the flexible nature of the intracellular region, most experimental data has focussed on the transmembrane and extracellular domains and therefore supports either model [ 76 , 77 ].…”

Section: Cellular Processes Mediated By Disordered Regions Binding Mementioning

confidence: 99%

Intrinsically disordered proteins and membranes: a marriage of convenience for cell signalling?

Cornish

Chamberlain

Owen

et al. 2020

Biochemical Society Transactions

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The structure-function paradigm has guided investigations into the molecules involved in cellular signalling for decades. The peripheries of this paradigm, however, start to unravel when considering the co-operation between proteins and the membrane in signalling processes. Intrinsically disordered regions hold distinct advantages over folded domains in terms of their binding promiscuity, sensitivity to their particular environment and their ease of modulation through post-translational modifications. Low sequence complexity and bias towards charged residues are also favourable for the multivalent electrostatic interactions that occur at the surfaces of lipid bilayers. This review looks at the principles behind the successful marriage between protein disorder and membranes in addition to the role of this partnership in modifying and regulating signalling in cellular processes. The HVR (hypervariable region) of small GTPases is highlighted as a well-studied example of the nuanced role a short intrinsically disordered region can play in the fine-tuning of signalling pathways.

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“…For the C1CRs, structures of the TMDs have been solved almost exclusively on group 1 members, i.e. PRLR [35], EPOR [75,76] and GHR [77] using detergent solubilized peptides and nuclear magnetic resonance (NMR) spectroscopy in both monomeric and dimeric states. However, monomeric structures have also been solved of the common receptor βc in bicelle membrane mimetics [78].…”

Section: Structural Biology Of C1crsmentioning

confidence: 99%

Orchestration of signaling by structural disorder in class 1 cytokine receptors

et al. 2020

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Background: Class 1 cytokine receptors (C1CRs) are single-pass transmembrane proteins responsible for transmitting signals between the outside and the inside of cells. Remarkably, they orchestrate key biological processes such as proliferation, differentiation, immunity and growth through long disordered intracellular domains (ICDs), but without having intrinsic kinase activity. Despite these key roles, their characteristics remain rudimentarily understood. Methods: The current paper asks the question of why disorder has evolved to govern signaling of C1CRs by reviewing the literature in combination with new sequence and biophysical analyses of chain properties across the family. Results: We uncover that the C1CR-ICDs are fully disordered and brimming with SLiMs. Many of these short linear motifs (SLiMs) are overlapping, jointly signifying a complex regulation of interactions, including network rewiring by isoforms. The C1CR-ICDs have unique properties that distinguish them from most IDPs and we forward the perception that the C1CR-ICDs are far from simple strings with constitutively bound kinases. Rather, they carry both organizational and operational features left uncovered within their disorder, including mechanisms and complexities of regulatory functions. Conclusions: Critically, the understanding of the fascinating ability of these long, completely disordered chains to orchestrate complex cellular signaling pathways is still in its infancy, and we urge a perceptional shift away from the current simplistic view towards uncovering their full functionalities and potential.

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Structural basis of the signal transduction via transmembrane domain of the human growth hormone receptor

Cited by 31 publications

References 51 publications

A twist in the ABC: regulation of ABC transporter trafficking and transport by FK506‐binding proteins

A twist in the ABC: regulation of ABC transporter trafficking and transport by FK506‐binding proteins

Intrinsically disordered proteins and membranes: a marriage of convenience for cell signalling?

Orchestration of signaling by structural disorder in class 1 cytokine receptors

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