Heterotypic interactions and sequence features modulate cellular reflectin condensate dynamics
- 1Soka University of America
Abstract
Reflectin proteins drive dynamic structural coloration in cephalopods by organizing into dense intracellular lamellar structures that dictate local refractive index. While reconstituted reflectins readily undergo liquid-liquid phase separation in vitro, these assemblies frequently undergo dynamic arrest, vitrifying into non-dynamic condensates. Here, we investigate how primary sequence features, post-translational modifications, and heterotypic interactions regulate the material properties of reflectin condensates within the environment of mammalian HeLa cells. Using confocal microscopy and fluorescence recovery after photobleaching (FRAP), we demonstrate that canonical block copolymeric A-type reflectins readily form dynamically arrested condensates, with the linker blocks primarily responsible for the observed arrest. In contrast, non-canonical B/C reflectin variants exhibit significantly greater fluidity and rapid recovery kinetics. We show that phosphomimetic substitutions progressively fluidize some reflectin condensates. Lastly, we find that heterotypic condensates composed of canonical and non-canonical reflectins in combinations associated with reversible iridescence in squid substantially enhance canonical mobility. Our findings establish a biophysical framework in which phosphorylation and heterotypic mixing cooperatively suppress dynamic arrest, enabling the reversible material transitions required for active cephalopod camouflage and communication.
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BibTeX
@misc{phan2026heterotypic,
title = {{Heterotypic interactions and sequence features modulate cellular reflectin condensate dynamics}},
author = {C. Phan and R. Watanabe and V. Q. Le and S. Walsh and R. Levenson},
howpublished = {bioRxiv},
year = {2026},
month = aug,
doi = {10.64898/2026.08.27.747642},
url = {https://www.biorxiv.org/content/10.64898/2026.08.27.747642v2},
note = {CC BY-ND},
}
RIS
TY - UNPB
TI - Heterotypic interactions and sequence features modulate cellular reflectin condensate dynamics
AU - C. Phan
AU - R. Watanabe
AU - V. Q. Le
AU - S. Walsh
AU - R. Levenson
PY - 2026
DA - 2026/08/27
PB - bioRxiv
DO - 10.64898/2026.08.27.747642
UR - https://www.biorxiv.org/content/10.64898/2026.08.27.747642v2
AB - Reflectin proteins drive dynamic structural coloration in cephalopods by organizing into dense intracellular lamellar structures that dictate local refractive index. While reconstituted reflectins readily undergo liquid-liquid phase separation in vitro, these assemblies frequently undergo dynamic arrest, vitrifying into non-dynamic condensates. Here, we investigate how primary sequence features, post-translational modifications, and heterotypic interactions regulate the material properties of reflectin condensates within the environment of mammalian HeLa cells. Using confocal microscopy and fluorescence recovery after photobleaching (FRAP), we demonstrate that canonical block copolymeric A-type reflectins readily form dynamically arrested condensates, with the linker blocks primarily responsible for the observed arrest. In contrast, non-canonical B/C reflectin variants exhibit significantly greater fluidity and rapid recovery kinetics. We show that phosphomimetic substitutions progressively fluidize some reflectin condensates. Lastly, we find that heterotypic condensates composed of canonical and non-canonical reflectins in combinations associated with reversible iridescence in squid substantially enhance canonical mobility. Our findings establish a biophysical framework in which phosphorylation and heterotypic mixing cooperatively suppress dynamic arrest, enabling the reversible material transitions required for active cephalopod camouflage and communication.
ER -