Evidence map›Paper›PMID 34049882›Full record

ArticleScience advances2021

Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin.

Antonio Sponga, Joan L Arolas, Thomas C Schwarz, Cy M Jeffries, Ariadna Rodriguez Chamorro, Julius Kostan, Andrea Ghisleni, Friedel Drepper, Anton Polyansky, Euripedes De Almeida Ribeiro and 17 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 26 citations in OpenAlex.

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  4. Accurate conformational ensembles of intrinsically disordered proteins using reweighting based on NMR chemical shifts.Proceedings of the National Academy of Sciences of the United States of America · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

27 authors at 7 institutions in 7 countries.

Antonio SpongaDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.ORCID 0000-0003-2216-4199
Joan L ArolasDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.ORCID 0000-0002-4198-5016
Thomas C SchwarzDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.ORCID 0000-0002-3812-9446
Cy M JeffriesEuropean Molecular Biology Laboratory (EMBL), Hamburg Unit, Hamburg, Germany.ORCID 0000-0002-8718-7343
Ariadna Rodriguez ChamorroDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.ORCID 0000-0002-2608-2425
Julius KostanDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.ORCID 0000-0002-8347-111X
Andrea GhisleniKing's College London BHF Centre for Research Excellence, Randall Centre for Cell and Molecular Biophysics, London SE1 1UL, UK.ORCID 0000-0001-8456-5903
Friedel DrepperBiochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany.ORCID 0000-0002-2043-5795
Anton PolyanskyDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Euripedes De Almeida RibeiroDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Miriam PedronDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.ORCID 0000-0003-1260-1420
Anna Zawadzka-KazimierczukBiological and Chemical Research Centre, Faculty of Chemistry, University of Warsaw, Zwirki i Wigury 101, 02-089 Warsaw, Poland.ORCID 0000-0002-1125-7923
Georg MlynekDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.ORCID 0000-0003-1454-4044
Thomas PeterbauerDepartment of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Dr. BohrGasse 9, A-1030 Vienna, Austria.
Pierantonio DotoDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Claudia SchreinerDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.ORCID 0000-0002-4206-6169
Eneda HollerlDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Borja MateosDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.ORCID 0000-0002-0310-4943
Leonhard GeistDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.ORCID 0000-0002-3241-676X
Georgine FaulknerDepartment of Biology, University of Padova, 35100 Padova, Italy.ORCID 0000-0003-1475-456X
Wiktor KozminskiBiological and Chemical Research Centre, Faculty of Chemistry, University of Warsaw, Zwirki i Wigury 101, 02-089 Warsaw, Poland.ORCID 0000-0003-2319-4525
Dmitri I SvergunKing's College London BHF Centre for Research Excellence, Randall Centre for Cell and Molecular Biophysics, London SE1 1UL, UK.ORCID 0000-0003-0830-5696
Bettina WarscheidBiochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany.ORCID 0000-0001-5096-1975
Bojan ZagrovicDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Mathias GautelKing's College London BHF Centre for Research Excellence, Randall Centre for Cell and Molecular Biophysics, London SE1 1UL, UK.ORCID 0000-0003-4027-9803
Robert KonratDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Kristina Djinović-CarugoDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria. kristina.djinovic@univie.ac.at.ORCID 0000-0003-0252-2972
University of Vienna · ATKing's College London · GBUniversity of Freiburg · DEUniversity of Warsaw · PLEuropean Molecular Biology Laboratory · DENational Research University Higher School of Economics · RUUniversity of Padua · IT

Funding

Austrian Science Fund FWF I 1593Austrian Science Fund FWF I 525Austrian Science Fund FWF P 30550Austrian Science Fund FWF W 1224British Heart Foundation CH/08/001/25300Wellcome Trust 201543/Z/16/Z
6 · The paper itself

Abstract

In sarcomeres, α-actinin cross-links actin filaments and anchors them to the Z-disk. FATZ (filamin-, α-actinin-, and telethonin-binding protein of the Z-disk) proteins interact with α-actinin and other core Z-disk proteins, contributing to myofibril assembly and maintenance. Here, we report the first structure and its cellular validation of α-actinin-2 in complex with a Z-disk partner, FATZ-1, which is best described as a conformational ensemble. We show that FATZ-1 forms a tight fuzzy complex with α-actinin-2 and propose an interaction mechanism via main molecular recognition elements and secondary binding sites. The obtained integrative model reveals a polar architecture of the complex which, in combination with FATZ-1 multivalent scaffold function, might organize interaction partners and stabilize α-actinin-2 preferential orientation in Z-disk. Last, we uncover FATZ-1 ability to phase-separate and form biomolecular condensates with α-actinin-2, raising the question whether FATZ proteins can create an interaction hub for Z-disk proteins through membraneless compartmentalization during myofibrillogenesis.

Identifiers

PMID34049882
PMCPMC8163081
OpenAlexW3165725385

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.