Intrinsically Disordered Regions of Human Plasma Membrane Proteins Preferentially Occur in the Cytoplasmic Segment

Minezaki, Yoshiaki; Homma, Keiichi; Nishikawa, Ken

doi:10.1016/j.jmb.2007.02.033

Cited by 95 publications

(95 citation statements)

References 78 publications

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“…Thus, membrane binding of ζ cyt , CD3ε cyt and FcεRγ cyt might prevent homo-oligomerization of these CYTO domains 9 in receptor clusters on the surface of resting cells and during random encounters of receptors diffusing in the cell membrane. Considering the reported prevalence of IDRs in the CYTO domains of many other human TM proteins, 7,8 one can expect that the distinctive features of the ITAM-containing IDRs observed in membrane binding studies 10,53 can be found for other CYTO IDRs, as well. Further studies will have to test this hypothesis of potential physiological significance.…”

Section: H-mentioning

confidence: 99%

“…Prevalence of IDRs in the CYTO domains of many human TM proteins in general, 7,8 and in particular, in the CYTO domains of signaling-related proteins (Table 1), 9,10,52 raises the question if these regions exert membrane-binding activity and if affirmed, whether this activity has a physiological role. Recent studies of the intrinsically disordered CYTO domains of the ζ and CD3ε signaling subunits (ζ cyt and CD3ε cyt , respectively) of the T cell receptor (TCR) have demonstrated that these proteins bind to acidic dimyristoylphosphatidylglycerol (DMPG) vesicles and undergo a helical folding transition upon binding.…”

Section: Protein Order Disorder and Oligomericity In Transmembramentioning

confidence: 99%

“…9,11 These findings are in line with the known dependence of the overall binding affinity between proteins on the function of the protein complex. For example, obligate homodimers are strongly associated proteins 7 and that protein phosphorylation predominantly occurs within IDRs, 6 further suggesting an important role of intrinsic disorder in receptor-mediated signaling.…”

Section: Receptor Signalingmentioning

confidence: 99%

“…6 In addition, long IDRs preferentially reside on the CYTO side of many human TM proteins. 7,8 In this context, the recently reported surprising ability of intrinsically disordered CYTO domains of immune receptor signaling subunits to form specific dimers [9][10][11] represents a functional link between protein intrinsic disorder and oligomericity. This phenomenon resolves a long-standing puzzle of receptor-mediated signaling and has important fundamental and clinical applications.…”

Section: Introductionmentioning

confidence: 99%

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The SCHOOL of nature: II. Protein order, disorder, and oligomericity in transmembrane signaling

Sigalov¹

2010

Self/Nonself

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Section: H-mentioning

confidence: 99%

Section: Protein Order Disorder and Oligomericity In Transmembramentioning

confidence: 99%

Section: Receptor Signalingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The SCHOOL of nature: II. Protein order, disorder, and oligomericity in transmembrane signaling

Sigalov¹

2010

Self/Nonself

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“…The relatively small number of available CD cell-surface markers (∼350) [29], compared to the number of predicted human transmembrane (∼13 000) [39,40] and PM proteins (∼2700) [40](see Fig. 3) illustrates the gap between the currently available cell-surface markers vs. potential markers.…”

Section: Challenges To Identifying New Cell-surface Markersmentioning

confidence: 99%

A novel role for proteomics in the discovery of cell‐surface markers on stem cells: Scratching the surface

Gundry

Boheler

Eyk

et al. 2008

Proteomics Clinical Apps

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The concept of cell-based therapy has been advocated as a novel approach for treating diseases or conditions where regeneration of cells, tissue and/or potentially organs is required. A promising source for cell-replacement therapies is provided by stem cells, but the success of this approach will ultimately rely on the ability to isolate primary stem or progenitor cells. Cell-surface protein markers will play a critical role in this step. Current methodologies for the identification of cell-surface protein markers rely primarily on antibody availability and flow cytometry, but many cell-surface proteins remain undetectable. Proteomic technologies now offer the possibility to specifically identify and investigate the cell-surface subproteome in a quantitative and discovery-driven manner. Once a cell surface protein marker panel has been identified by MS and the antibodies become available, the panel should permit the identification, tracking, and/or isolation of stem or progenitor cells that may be appropriate for therapeutics. This review provides a context for the use of proteomics in discovering new cell-surface markers for stem cells.

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The Un(f)told Story of General Anesthesia

Zsila

2018

ChemBioChem

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Inhalational anesthetics are routinely employed in clinical practice to accomplish general anesthesia. Concerns have recently emerged regarding the deleterious impact of these volatile agents on cognitive performance, immune functions, and tumor recurrence and metastasis. These agents have been shown to modify the gene-expression pattern as well as cell signaling in tumor cells, but the underlying molecular mechanisms remain a matter of conjecture. Regulatory/signaling proteins either of cytosolic or membrane origin abundantly contain intrinsically disordered sequences, the conformational pliability of which is pivotal in their biological functions. It is well known that chloroform (an anesthetic itself), trifluoroethanol, hexafluoroisopropanol, and related haloalcohols markedly affect the structure of disordered proteins and protein regions by inducing folding, misfolding, or even aggregation. Taking into consideration the physicochemical similarities and protein interaction modes of these volatile solvents and inhaled anesthetics, it is postulated that administration of these drugs can also modify the secondary structure of disordered protein segments. Accordingly, pharmacological effects of anesthetics may, at least in part, be mediated by conformational perturbations of intrinsic disorder-based regulatory protein networks of cells.

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Intrinsically Disordered Regions of Human Plasma Membrane Proteins Preferentially Occur in the Cytoplasmic Segment

Cited by 95 publications

References 78 publications

The SCHOOL of nature: II. Protein order, disorder, and oligomericity in transmembrane signaling

The SCHOOL of nature: II. Protein order, disorder, and oligomericity in transmembrane signaling

A novel role for proteomics in the discovery of cell‐surface markers on stem cells: Scratching the surface

The Un(f)told Story of General Anesthesia

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