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A de novo missense variant in MIDEAS results in increased deacetylase activity of the MiDAC HDAC complex causing a neurodevelopmental syndrome

The MiDAC complex regulates gene expression through histone deacetylation. Here, the authors identify a recurrent MIDEAS mutation that disrupts an auto-inhibitory loop, elevating deacetylase activity and causing a multisystem developmental disorder.

Louise Fairall
Kristupas Sirvydis
John WR Schwabe
ResearchOpen Access25 Nov 2025
Nature Communications

Volume: 16, P: 1-14
Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate

The core FADD:Caspase-8 complex and its regulatory partners, such as the cell death inhibitor c-FLIP, coordinate cell fate. Here authors present the structure of full-length procaspase-8 in a complex with FADD and reveal how recruitment of c-FLIP_S into this complex inhibits Caspase-8 activity.

Joanna L. Fox
Michelle A. Hughes
Marion MacFarlane
ResearchOpen Access05 Feb 2021
Nature Communications

Volume: 12, P: 1-17
Remodelling of a polypyrimidine tract-binding protein complex during apoptosis activates cellular IRESs

H A King
L C Cobbold
A E Willis
ResearchOpen Access18 Oct 2013
Cell Death & Differentiation

Volume: 21, P: 161-171
XLS (c9orf142) is a new component of mammalian DNA double-stranded break repair

A Craxton
J Somers
M Malewicz
ResearchOpen Access13 Mar 2015
Cell Death & Differentiation

Volume: 22, P: 890-897
Characterization of novel markers of senescence and their prognostic potential in cancer

M Althubiti
L Lezina
S Macip
ResearchOpen Access20 Nov 2014
Cell Death & Disease

Volume: 5, P: e1528

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A de novo missense variant in MIDEAS results in increased deacetylase activity of the MiDAC HDAC complex causing a neurodevelopmental syndrome

Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate

Remodelling of a polypyrimidine tract-binding protein complex during apoptosis activates cellular IRESs

XLS (c9orf142) is a new component of mammalian DNA double-stranded break repair

Characterization of novel markers of senescence and their prognostic potential in cancer

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