TY - JOUR
AU - Sponga, Antonio
AU - Arolas, Joan L.
AU - Schwarz, Thomas C.
AU - Jeffries, Cy M.
AU - Rodriguez Chamorro, Ariadna
AU - Kostan, Julius
AU - Ghisleni, Andrea
AU - Drepper, Friedel
AU - Polyansky, Anton
AU - De Almeida Ribeiro, Euripedes
AU - Pedron, Miriam
AU - Zawadzka-Kazimierczuk, Anna
AU - Mlynek, Georg
AU - Peterbauer, Thomas
AU - Doto, Pierantonio
AU - Schreiner, Claudia
AU - Hollerl, Eneda
AU - Mateos, Borja
AU - Geist, Leonhard
AU - Faulkner, Georgine
AU - Kozminski, Wiktor
AU - Svergun, Dmitri I.
AU - Warscheid, Bettina
AU - Zagrovic, Bojan
AU - Gautel, Mathias
AU - Konrat, Robert
AU - Djinović-Carugo, Kristina
TI - Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin
JO - Science advances
VL - 7
IS - 22
SN - 2375-2548
CY - Washington, DC [u.a.]
PB - Assoc.
M1 - PUBDB-2021-02832
SP - eabg7653 -
PY - 2021
AB - 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.
LB - PUB:(DE-HGF)16
C6 - pmid:34049882
UR - <Go to ISI:>//WOS:000655906900037
DO - DOI:10.1126/sciadv.abg7653
UR - https://bib-pubdb1.desy.de/record/459946
ER -