Ionic Interactions Promote Transmembrane Helix–Helix Association Depending on Sequence Context

Herrmann, Jana; Fuchs, Angelika; Panitz, Johanna C.; Eckert, Thomas; Unterreitmeier, Stephanie; Frishman, Dmitrij; Langosch, Dieter

doi:10.1016/j.jmb.2009.11.054

Cited by 26 publications

(33 citation statements)

References 47 publications

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“…Table 1 compares the primary structure of the N-terminal stretch of human type-1 VDAC/porin with that of the amyloid Ab peptide Ab1-42, and thus demonstrates that either peptide includes at least one GxxxG motif, putatively working as a peptide aggregation/ membrane perturbation sequence. What might be worth to mention, my laboratory has also presented data indicating that the GxxxG motif at the N-terminal peptide works as an ATP-binding site [3][4][5][6][7]. However, the data support a new way to look at the pathogenesis of Alzheimers disease and the induction of apoptosis [8].…”

mentioning

confidence: 99%

Apoptogenic interactions of plasmalemmal type-1 VDAC and Aβ peptides via GxxxG motifs induce Alzheimer's disease – a basic model of apoptosis?*

Thinnes¹

2011

Wien Med Wochenschr

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Human type-1 porin/VDAC (voltage-dependent anion channel) carries a GxxxG motif in its N-terminal part, traversing the β-barrel, while the Alzheimer's disease (AD) relevant amyloid peptides Aβ1-42 and Aβ1-40 show a series of corresponding motifs close to their C-terminus. GxxxG motifs are established as aggregation/membrane perturbation motifs. These peptide primary structure data support a proposal I recently made on the basis of a synopsis of recent literature. Accordingly, amyloid Aβ, cut from APP by beta-secretase BACE1 and gamma-secretase, has been insinuated to induce Alzheimer's disease via apoptosis by opening type-1 porin/VDAC in cell membranes of hypometabolic neuronal cells. Considering the ubiquitous expression modus of APP, beta- and gamma-secretases and type-1 VDAC/eukaryotic porin a basic model of apoptosis might be given.

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mentioning

confidence: 99%

Apoptogenic interactions of plasmalemmal type-1 VDAC and Aβ peptides via GxxxG motifs induce Alzheimer's disease – a basic model of apoptosis?*

Thinnes¹

2011

Wien Med Wochenschr

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“…And, it has to be stressed that residues adjacent to a sequence motif also contribute to the interactions. [45][46][47][48] (3) Associations between helical TM domains are dynamic by nature. Different types of motion of TM α helices have been described: lateral translation, piston, rotation parallel to the membrane (pivot or tilt) and rotation perpendicular to the membrane.…”

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confidence: 99%

Single-spanning transmembrane domains in cell growth and cell-cell interactions

Hubert

Sawma

Duneau

et al. 2010

Cell Adhesion & Migration

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“…To validate BLaTM for heterotypic TMD-TMD interactions, we employed the LS46 model TMD previously isolated from a combinatorial library32. Using the ToxR assay, it had been shown that LS46 shows strong homotypic interaction.…”

Section: Resultsmentioning

confidence: 99%

“…These analyses uncovered the importance of interfacial GxxxG22, QxxS23, and serine/threonine-containing24 motifs as well as aromatic252627 and carboxamide2829 residues. Library screens also produced more complex motifs where phenylalanine30, histidine/serine/threonine31 or ionizable residues32 combine with GxxxG motifs to form strong self-interaction.…”

mentioning

confidence: 99%

Identifying ionic interactions within a membrane using BLaTM, a genetic tool to measure homo- and heterotypic transmembrane helix-helix interactions

Schanzenbach

Schmidt

Breckner

et al. 2017

Sci Rep

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The assembly of integral membrane protein complexes is frequently supported by transmembrane domain (TMD) interactions. Here, we present the BLaTM assay that measures homotypic as well as heterotypic TMD-TMD interactions in a bacterial membrane. The system is based on complementation of β-lactamase fragments genetically fused to interacting TMDs, which confers ampicillin resistance to expressing cells. We validated BLaTM by showing that the assay faithfully reports known sequence-specific interactions of both types. In a practical application, we used BLaTM to screen a focussed combinatorial library for heterotypic interactions driven by electrostatic forces. The results reveal novel patterns of ionizable amino acids within the isolated TMD pairs. Those patterns indicate that formation of heterotypic TMD pairs is most efficiently supported by closely spaced ionizable residues of opposite charge. In addition, TMD heteromerization can apparently be driven by hydrogen bonding between basic or between acidic residues.

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Ionic Interactions Promote Transmembrane Helix–Helix Association Depending on Sequence Context

Cited by 26 publications

References 47 publications

Apoptogenic interactions of plasmalemmal type-1 VDAC and Aβ peptides via GxxxG motifs induce Alzheimer's disease – a basic model of apoptosis?*

Apoptogenic interactions of plasmalemmal type-1 VDAC and Aβ peptides via GxxxG motifs induce Alzheimer's disease – a basic model of apoptosis?*

Single-spanning transmembrane domains in cell growth and cell-cell interactions

Identifying ionic interactions within a membrane using BLaTM, a genetic tool to measure homo- and heterotypic transmembrane helix-helix interactions

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