Fig. 1: NEMO is associated with pathological protein aggregates. | Nature Communications

Fig. 1: NEMO is associated with pathological protein aggregates.

From: NEMO reshapes the α-Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62

Fig. 1

a Widespread mixed brain proteinopathy in a patient expressing mutant Q330X NEMO. Both low and high magnification images show the presence of aggregated proteins, such as α-synuclein, hyperphosphorylated tau, TDP-43, and amyloid beta in different brain regions. Many structures resembling Lewy body and Lewy neurites in pigmented neurons in the substantia nigra pars compacta (SNpc) are positive in immunostaining for α-synuclein, hyperphosphorylated tau, and ubiquitin. Scale bars, as indicated. b Domain structure of wildtype (WT) human NEMO and mutant Q330X NEMO. DD dimerization ___domain, CC1 coiled-coil 1 ___domain, CC2 coiled-coil 2 ___domain, UBAN ubiquitin-binding in ABIN and NEMO, LZ leucine zipper, ZF zinc finger. c, d M1-linked ubiquitin and NEMO co-localize with α-synuclein, tau, and TDP-43 aggregates in human brain. Immunofluorescent stainings of cortical or midbrain sections from patients with Parkinson’s disease (PD), Alzheimer´s disease (AD), or frontotemporal dementia (FTD). Brain sections were stained with antibodies against M1-ubiquitin (c), NEMO (d), and α-synuclein (PD), tau (AD), or TDP-43 (FTD); DAPI (blue). Scale bar, 10 µm.

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