Carolin Koerner

Max Planck Institute of Molecular Physiology

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Alfred Wittinghofer

Max Planck Institute of Molecular Physiology

A. Wittinghofer

Max Planck Institute of Molecular Physiology

Andrea Musacchio

Max Planck Institute of Molecular Physiology

I.R. Vetter

Ludwig-Maximilians-Universität München

M. Miertzschke

Volker Hickmann

BASF (Germany)

Mandy Miertzschke

Max Planck Institute of Molecular Physiology

Sabine Wohlgemuth

Max Planck Institute of Molecular Physiology

Pim J. Huis in ’t Veld

Max Planck Institute of Molecular Physiology

Katja Gotthardt

Max Planck Institute of Molecular Physiology

Cooperative Institutions

Max Planck Institute of Molecular Physiology

Max Planck Society

University of Bonn

University Hospital Bonn

European Molecular Biology Laboratory

Sapienza University of Rome

National Research Council

Howard Hughes Medical Institute

Ludwig-Maximilians-Universität München

Leiden University

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609 ADHESION OF NATURAL KILLER (NK) CELLS TO EXTRACELLULAR MATRIX IS CRITICALLY REGULATED BY HCV 2/CD81 INTERACTIONS

Journal of Hepatology (2008)

Bjoern F. Kraemer Dominik M. Schulte C Zwank Carolin Koerner M. Neibecker

CD81

10.1016/s0168-8278(08)60611-x

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Citations (0)

A Validation Strategy to Assess the Role of Phase Separation as Determinant of Macromolecular Localization

Marius Hedtfeld Alicia Dammers Carolin Koerner Andrea Musacchio

Liquid-liquid phase separation (LLPS) is considered a general mechanism for assembling macromolecular compartments. LLPS assays with single macromolecules (homotypic) are often used to identify phase separation scaffolds. The predictive value of these assays for compartment assembly, however, remains poorly characterized. The chromosomal passenger complex (CPC) promotes chromosome biorientation. Its chromosome recruitment requires specific phosphomarks, but recent studies also identified LLPS as trigger of CPC chromosome enrichment. Here, we show that correctly localizing CPC and variants failing to localize in vivo have indistinguishable in vitro LLPS propensities. Despite successful mixing in vitro with localization-proficient CPC, these variants fail to localize even in presence of endogenous CPC, thus excluding defective LLPS nucleation as cause of mislocalization. In vitro, LLPS of the CPC was enhanced by commonly used crowding agents but effectively inhibited by cytomimetic conditions. Besides shedding new light on CPC recruitment, our results showcase a validation pipeline to assess disputed roles of LLPS in the assembly of other cellular compartments.

Separation (statistics)

10.2139/ssrn.4472737

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Author Index

Journal of Biological Chemistry (2018)

Abou Hassan Johannes M. F. G. Aerts A. Chiara John Andrew Jesusa M.G. Arevalo

10.1016/s0021-9258(20)33836-9

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The Interaction of CCDC104/BARTL1 with Arl3 and Implications for Ciliary Function

Structure (2015)

Mandy Lokaj Stefanie Kristine Kösling Carolin Koerner Sven M. Lange Sylvia E. C. van Beersum

Cilia are small antenna-like cellular protrusions critical for many developmental signaling pathways. The ciliary protein Arl3 has been shown to act as a specific release factor for myristoylated and farnesylated ciliary cargo molecules by binding to the effectors Unc119 and PDE6δ. Here we describe a newly identified Arl3 binding partner, CCDC104/CFAP36. Biochemical and structural analyses reveal that the protein contains a BART-like domain and is called BARTL1. It recognizes an LLxILxxL motif at the N-terminal amphipathic helix of Arl3, which is crucial for the interaction with the BART-like domain but also for the ciliary localization of Arl3 itself. These results seem to suggest a ciliary role of BARTL1, and possibly link it to the Arl3 transport network. We thus speculate on a regulatory mechanism whereby BARTL1 aids the presentation of active Arl3 to its GTPase-activating protein RP2 or hinders Arl3 membrane binding in the area of the transition zone.

Small GTPase

10.1016/j.str.2015.08.016

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Citations (26)

RasGEF1A and RasGEF1B are guanine nucleotide exchange factors that discriminate between Rap GTP‐binding proteins and mediate Rap2‐specific nucleotide exchange

FEBS Journal (2009)

Elif Yaman Raphael Gasper Carolin Koerner Alfred Wittinghofer Uygar Halis Tazebay

The highly conserved RasGEF1 family of proteins contain a C‐terminal CDC25‐Ras exchange motif domain and an N‐terminal RasGEF‐N domain, and are of unknown function and specificity. Using purified RasGEF1A and RasGEF1B proteins, as well as Ras family proteins, we established that RasGEF1A and RasGEF1B function as very specific exchange factors for Rap2, a member of the Rap subfamily of Ras‐like G‐proteins. They do not act on Rap1 or other members of the Ras subfamily. Although Rap2 was implicated in the regulation of cell adhesion, the establishment of cell morphology, and the modulation of synapses in neurons, no specific guanine nucleotide exchange factor for Rap2 was previously identified. Using reciprocal site‐directed mutagenesis, we analyzed residues that allow RasGEF1 proteins to discriminate between Rap1 and Rap2, and we were able to identify Phe39 in the switch I region of Rap2 as a specificity residue. Mutation of the corresponding Ser39 in Rap1 changed the specificity and allowed the nucleotide exchange of Rap1(S39F) to be stimulated by RasGEF1B.

Rap1

Subfamily

GTP-binding protein regulators

10.1111/j.1742-4658.2009.07166.x

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Citations (35)

Crystal structure of Ran-GPPNHP-RanBP1-RanGAP complex

Michael J. Seewald Carolin Koerner A. Wittinghofer I.R. Vetter

Ran

10.2210/pdb1k5d/pdb

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Reconstitution and use of highly active human CDK1:Cyclin-B:CKS1 complexes

bioRxiv (Cold Spring Harbor Laboratory) (2021)

Pim J. Huis in ’t Veld Sabine Wohlgemuth Carolin Koerner Franziska Mueller Petra Janning

Abstract As dividing cells transition into mitosis, hundreds of proteins are phosphorylated by a complex of cyclin-dependent kinase 1 (CDK1) and Cyclin-B, often at multiple sites. CDK1:Cyclin-B phosphorylation patterns alter conformations, interaction partners, and enzymatic activities and need to be recapitulated in vitro for the structural and functional characterization of the mitotic protein machinery. This requires a pure and active recombinant kinase complex. The kinase activity of CDK1 critically depends on the phosphorylation of a Threonine residue in its activation loop by a CDK1 activating kinase (CAK). We developed protocols to activate CDK1:Cyclin-B either in vitro with purified CDK1 activating kinases (CAK) or in insect cells through CDK-CAK co-expression. To boost kinase processivity, we reconstituted a tripartite complex consisting of CDK1, Cyclin-B, and CKS1. In this work, we provide and compare detailed protocols to obtain and use highly active CDK1:Cyclin-B (CC) and CDK1:Cyclin-B:CKS1 (CCC).

Cyclin-dependent kinase complex

Cyclin B

Cyclin A

Cyclin B1

Cyclin A2

10.1101/2021.09.24.461690

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Citations (2)

Sulfolobus solfataricus SWI2/SNF2 ATPase C-terminal domain

H. DUERR Carolin Koerner Martin J. Mueller Volker Hickmann Karl‐Peter Hopfner

Sulfolobus solfataricus

10.2210/pdb1z5z/pdb

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Structural insights into the small G-protein Arl13B and implications for Joubert syndrome

Biochemical Journal (2013)

Mandy Miertzschke Carolin Koerner Michael Spoerner Alfred Wittinghofer

Ciliopathies are human diseases arising from defects in primary or motile cilia. The small G-protein Arl13B (ADP-ribosylation factor-like 13B) localizes to microtubule doublets of the ciliary axoneme and is mutated in Joubert syndrome. Its GDP/GTP mechanistic cycle and the effect of its mutations in patients with Joubert syndrome remain elusive. In the present study we applied high resolution structural and biochemical approaches to study Arl13B. The crystal structure of Chlamydomonas rheinhardtii Arl13B, comprising the G-domain and part of its unique C-terminus, revealed an incomplete active site, and together with biochemical data the present study accounts for the absence of intrinsic GTP hydrolysis by this protein. The structure shows that the residues representing patient mutations R79Q and R200C are involved in stabilizing important intramolecular interactions. Our studies suggest that Arg79 is crucial for the GDP/GTP conformational change by stabilizing the large two-residue register shift typical for Arf (ADP-ribosylation factor) and Arl subfamily proteins. A corresponding mutation in Arl3 induces considerable defects in effector and GAP (GTPase-activating protein) binding, suggesting a loss of Arl13B function in patients with Joubert syndrome.

Joubert syndrome

ADP ribosylation factor

Axoneme

10.1042/bj20131097

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Citations (45)

Reconstitution and use of highly active human CDK1:Cyclin‐B:CKS1 complexes

Protein Science (2021)

Pim J. Huis in ’t Veld Sabine Wohlgemuth Carolin Koerner Franziska Müller Petra Janning

As dividing cells transition into mitosis, hundreds of proteins are phosphorylated by a complex of cyclin-dependent kinase 1 (CDK1) and Cyclin-B, often at multiple sites. CDK1:Cyclin-B phosphorylation patterns alter conformations, interaction partners, and enzymatic activities of target proteins and need to be recapitulated in vitro for the structural and functional characterization of the mitotic protein machinery. This requires a pure and active recombinant kinase complex. The kinase activity of CDK1 critically depends on the phosphorylation of a Threonine residue in its activation loop by a CDK1-activating kinase (CAK). We developed protocols to activate CDK1:Cyclin-B either in vitro with purified CAKs or in insect cells through CDK-CAK co-expression. To boost kinase processivity, we reconstituted a ternary complex consisting of CDK1, Cyclin-B, and CKS1. In this work, we provide and compare detailed protocols to obtain and use highly active CDK1:Cyclin-B (CC) and CDK1:Cyclin-B:CKS1 (CCC).

Cyclin-dependent kinase complex

Cyclin B

Cyclin B1

10.1002/pro.4233

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Citations (18)