Dorith Wunnicke

A short intrinsically disordered region at KtrB’s N-terminus facilitates allosteric regulation of K+ channel KtrAB

Janina Stautz, David Griwatz, Susann Kaltwasser, Ahmad Reza Mehdipour et autres

homeostasis is crucial for bacterial survival. The bacterial K+ channel KtrAB is regulated by the binding of ADP and ATP to the cytosolic RCK subunits KtrA. While the ligand-induced conformational changes in KtrA are well described, the transmission to the gating regions …

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Inhibited KdpFABC transitions into an E1 off-cycle state

Jakob M. Silberberg, Charlott Stock, Lisa Hielkema, Robin Adam Corey et autres

KdpFABC is a high-affinity prokaryotic K + uptake system that forms a functional chimera between a channel-like subunit (KdpA) and a P-type ATPase (KdpB). At high K + levels, KdpFABC needs to be inhibited to prevent excessive K + accumulation to the …

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Author response: Inhibited KdpFABC transitions into an E1 off-cycle state

Jakob M. Silberberg, Charlott Stock, Lisa Hielkema, Robin Adam Corey et autres

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Inhibited KdpFABC resides in an E1 off-cycle state

Jakob M. Silberberg, Charlott Stock, Lisa Hielkema, Robin Adam Corey et autres

Abstract KdpFABC is a high-affinity prokaryotic K + uptake system that forms a functional chimera between a channel-like subunit (KdpA) and a P-type ATPase (KdpB). At high K + levels, KdpFABC needs to be inhibited to prevent excessive K + accumulation to …

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Regulation of lipid saturation without sensing membrane fluidity

Stephanie Ballweg, Erdinç Sezgin, Milka Doktorova, Roberto Covino et autres

Cells maintain membrane fluidity by regulating lipid saturation, but the molecular mechanisms of this homeoviscous adaptation remain poorly understood. We have reconstituted the core machinery for regulating lipid saturation in baker's yeast to study its molecular mechanism. By combining molecular dynamics simulations …

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How RCK domains regulate gating of K + channels

Marina Schrecker, Dorith Wunnicke, Inga Hänelt

Potassium channels play a crucial role in the physiology of all living organisms. They maintain the membrane potential and are involved in electrical signaling, pH homeostasis, cell-cell communication and survival under osmotic stress. Many prokaryotic potassium channels and members of the eukaryotic …

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Regulation of lipid saturation without sensing membrane fluidity

Stephanie Ballweg, Erdinç Sezgin, Dorith Wunnicke, Inga Hänelt et autres

Abstract/Summary Cells maintain membrane fluidity by regulating lipid saturation, but the molecular mechanisms of this homeoviscous adaptation remain poorly understood. Here, we have reconstituted the core machinery for sensing and regulating lipid saturation in baker’s yeast to directly characterize its response to …

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The KdpFABC Complex: What Happens When a P-Type ATPase Hijacks an Ion Channel

Charlott Stock, Lisa Hielkema, Igor Tascón, Dorith Wunnicke et autres

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Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels

Charlott Stock, Lisa Hielkema, Igor Tascón, Dorith Wunnicke et autres

Abstract P-type ATPases ubiquitously pump cations across biological membranes to maintain vital ion gradients. Among those, the chimeric K + uptake system KdpFABC is unique. While ATP hydrolysis is accomplished by the P-type ATPase subunit KdpB, K + has been assumed to …

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Allosteric Control of the K+ Uptake System KtrAB

Marina Diskowski, Vedrana Mikušević, Dorith Wunnicke, Ahmed R. Mehdipour et autres

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Activation of the Unfolded Protein Response by Lipid Bilayer Stress

Kristina Halbleib, Kristina Pesek, Roberto Covino, Harald F. Hofbauer et autres

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Helical jackknives control the gates of the double-pore K+ uptake system KtrAB

Marina Diskowski, Ahmad Reza Mehdipour, Dorith Wunnicke, Deryck J. Mills et autres

Ion channel gating is essential for cellular homeostasis and is tightly controlled. In some eukaryotic and most bacterial ligand-gated K+ channels, RCK domains regulate ion fluxes. Until now, a single regulatory mechanism has been proposed for all RCK-regulated channels, involving signal transduction …

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