Fig. 5: Hypothesis of hnRNPA1 forming different structures to adapt to different function. | Nature Communications

Fig. 5: Hypothesis of hnRNPA1 forming different structures to adapt to different function.

From: The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure

Fig. 5

a Domain organization of hnRNPA1. The LC domain is colored in green and zoomed in. Segment 251–295 that is involved in the the irreversible fibril core (FC) is colored in gray. The PY-NLS (segment 263–289) is highlighted in black. The reversible amyloid-forming core segments (RACs) are highlighted in yellow. b Schematic illustration of the different structural states of hnRNPA1. HnRNPA1 monomer forms complex with Kapβ2 via PY-NLS. In the state of phase separation, the LC domain play a major role in mediating self-association of hnRNPA1 for liquid–liquid phase separation (LLPS) and reversible amyloid fibril formation. Under disease conditions, hnRNPA1 further assembles into irreversible amyloid fibrils via PY-NLS.

Back to article page