Marta Carroni

Stockholm University

marta.carroni@scilifelab.se

+468162220

Keywords

AAA+, ATPaces, cryo-EM, Cryo-et, HSP 100 chaperones, protein quality control

Key publications

The structure of neurofibromin isoform 2 reveals different functional states
Naschberger A, Baradaran R, Rupp B, Carroni M*
Nature, 2021, Research article, https://doi.org/10.1038/s41586-021-04024-x
*Shared corresponding author

Antibacterial peptide CyclomarinA creates toxicity by deregulating the Mycobacterium tuberculosis ClpC1-ClpP1P2 protease
Taylor G, Frommherz Y, Katikaridis P, Layer D, Sinning I, Carroni M, Weber-Ban E, Mogk A.J
Biol Chem. 2022 Jun 26;298(8):102202. doi: 10.1016/j.jbc.2022.102202. Online ahead of print.PMID: 35768046

Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control
Carroni* M, Franke KB, Maurer M, Jäger J, Hantke I, Gloge F, Linder D, Gremer S, Turgay K, Bukau B, Mogk A.
Elife. 2017 Nov 22;6. pii: e30120. doi: 10.7554/eLife.30120.
*Shared corresponding author

Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase
Deville C*, Carroni M*, Franke KB, Topf M, Bukau B, Mogk A, Saibil HR.
Sci. Adv. 2017 Aug 3:8e1701726 doi: 10.1126/sciadv.1701726
*contributed equally

Human Hsp70 Disaggregase Reverses Parkinson’s-Linked α-Synuclein Amyloid Fibrils
Gao X, Carroni M, Nussbaum-Krammer C, Mogk A, Nillegoda NB, Szlachcic A, Guilbride DL, Saibil HR, Mayer MP, Bukau B.
Mol Cell. 2015 Sep 3;59(5):781-93. doi: 10.1016/j.molcel.2015.07.012.

Head-to-tail interactions of the coiled-coil domains regulate ClpB cooperation with Hsp70 in protein disaggregation
Carroni M., Kummer E., Oguchi Y., Wendler P., Clare D.K., Sinning I., Kopp J., Mogk A., Bukau B. and Saibil H.
Elife, 2014 Apr 30;3:e02481. doi: 10.7554/eLife.02481.

SciLifeLab / Contact / Marta Carroni

In our group, we use mainly cryo-EM to discover molecular regulatory mechanisms. We combine the technique also with cryogenic electron tomography (cryo-ET) and work at developing combinatory methods with fluorescence microscopy. We follow two main lines of research.

In the first one, we aim at understing the molecular mechanics of AAA+ proteins involved in cellular protein quality control. AAA+ are fascinating systems as they can perform extremely different tasks in the cell while sharing the same basic structural fold. We look into the special structural inserts and interaction with adaptor proteins that confer AAA+ chaperones resistance to stress in both bacteria and humans.

In a second line of research we use cryo-EM as a tool for longitudinal epitope mapping of antibody response in animal models and humans with the aim of gaining insights useful for better vaccine design or for understanding autoimmune diseases.

The group works in close proximity to the cryo-EM national unit at SciLifeLab, which I also supervise.

Group members

Stavros Azinas, postdoctoral fellow
Lisa Engelhardt, PhD student