Cyril Hanus

Institut de Psychiatrie et Neurosciences de Paris

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Mateusz Sikora

Max Planck Institute of Biophysics

Sören von Bülow

Max Planck Institute of Biophysics

Gerhard Hummer

Max Planck Institute of Biophysics

Michael Gecht

Max Planck Institute of Biophysics

Camille Penet

Institut de Psychiatrie et Neurosciences de Paris

Bertram Daum

University of Exeter

Erin M. Schuman

Max Planck Institute for Brain Research

Michail N. Isupov

University of Exeter

Matthew C. Gaines

University of Exeter

Klaus Reuter

Max Planck Computing and Data Facility

Cooperative Institutions

Max Planck Society

Max Planck Institute for Brain Research

Goethe University Frankfurt

Inserm

Centre National de la Recherche Scientifique

University of Exeter

Université Paris Cité

Max Planck Institute of Biophysics

Institut de Psychiatrie et Neurosciences de Paris

Institute of Biological Chemistry, Academia Sinica

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Synaptic Control of Secretory Trafficking in Dendrites

Cell Reports (2014)

Cyril Hanus Lisa Kochen Susanne tom Dieck Victor Racine Jean‐Baptiste Sibarita

Localized signaling in neuronal dendrites requires tight spatial control of membrane composition. Upon initial synthesis, nascent secretory cargo in dendrites exits the endoplasmic reticulum (ER) from local zones of ER complexity that are spatially coupled to post-ER compartments. Although newly synthesized membrane proteins can be processed locally, the mechanisms that control the spatial range of secretory cargo transport in dendritic segments are unknown. Here, we monitored the dynamics of nascent membrane proteins in dendritic post-ER compartments under regimes of low or increased neuronal activity. In response to activity blockade, post-ER carriers are highly mobile and are transported over long distances. Conversely, increasing synaptic activity dramatically restricts the spatial scale of post-ER trafficking along dendrites. This activity-induced confinement of secretory cargo requires site-specific phosphorylation of the kinesin motor KIF17 by Ca2+/calmodulin-dependent protein kinases (CaMK). Thus, the length scales of early secretory trafficking in dendrites are tuned by activity-dependent regulation of microtubule-dependent transport.

Kinesin

Secretory protein

Transport protein

10.1016/j.celrep.2014.05.028

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Citations (64)

Multiple Association States between Glycine Receptors and Gephyrin Identified by SPT Analysis

Biophysical Journal (2007)

Marie-Virginie Ehrensperger Cyril Hanus Christian Vannier Antoine Triller Maxime Dahan

Gephyrin

10.1529/biophysj.106.095596

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Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries

Cell (2024)

Yu-Xi Tsai Ning-En Chang Klaus Reuter Hao‐Ting Chang Tzu‐Jing Yang

Most membrane proteins are modified by covalent addition of complex sugars through N- and O-glycosylation. Unlike proteins, glycans do not typically adopt specific secondary structures and remain very mobile, shielding potentially large fractions of protein surface. High glycan conformational freedom hinders complete structural elucidation of glycoproteins. Computer simulations may be used to model glycosylated proteins but require hundreds of thousands of computing hours on supercomputers, thus limiting routine use. Here, we describe GlycoSHIELD, a reductionist method that can be implemented on personal computers to graft realistic ensembles of glycan conformers onto static protein structures in minutes. Using molecular dynamics simulation, small-angle X-ray scattering, cryoelectron microscopy, and mass spectrometry, we show that this open-access toolkit provides enhanced models of glycoprotein structures. Focusing on N-cadherin, human coronavirus spike proteins, and gamma-aminobutyric acid receptors, we show that GlycoSHIELD can shed light on the impact of glycans on the conformation and activity of complex glycoproteins.

Conformational isomerism

Membrane glycoproteins

10.1016/j.cell.2024.01.034

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CryoEM reveals the structure of an archaeal pilus involved in twitching motility.

Research Square (Research Square) (2023)

Bertram Daum Mathew Gaines Shamphavi Sivabalasarma Michail N. Isupov Risat Ul Haque

Abstract Amongst the major archaeal filament types, several have been shown to closely resemble bacterial homologues of the Type IV pili (T4P). Within Sulfolobales, member species encode for three types of T4P, namely the archaellum, the UV-inducible pilus (Uvp) and the archaeal adhesive pilus (Aap). Whereas the archaellum functions primarily in swimming motility, and the Uvp in UV-induced cell aggregation and DNA-exchange, the Aap plays an important role in adhesion and twitching motility. All previously solved Aap appear to have almost identical helical structures. Here, we present a cryoEM structure of the Aap of the archaeal model organism Sulfolobus acidocaldarius. We identify the component subunit as AapB and find that while its structure follows the canonical T4P blueprint, it adopts three distinct conformations within the pilus. The tri-conformer Aap structure that we describe challenges our current understanding of pilus structure and sheds new light on the principles of twitching motility.

Sulfolobus acidocaldarius

10.21203/rs.3.rs-3245295/v1

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One of the two N-glycans on the human Gb3/CD77 synthase is essential for its activity and allosterically regulates its function

Biochemical and Biophysical Research Communications (2022)

Krzysztof Mikołajczyk Mateusz Sikora Cyril Hanus Radosław Kaczmarek Marcin Czerwiński

10.1016/j.bbrc.2022.05.085

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Citations (6)

SnapShot: Local Protein Translation

Cyril Hanus Erin M. Schuman