Genetic manipulation of the optical refractive index in living cells

Ogawa, Junko; Iwata, Yoko; Tonnu, Nina; Gopinath, Chitra; Huang, Ling; Itoh, Susumu; Ando, Ryoko; Miyawaki, Atsushi; Verma, Inder M.; Pao, Gerald M.

doi:10.1101/2020.07.09.196436

Cited by 5 publications

(8 citation statements)

References 14 publications

(10 reference statements)

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“…After transfection, reflectins were found to phase out from the crowded intracellular milieu, similar to what Atrouli (Chatterjee, Cerna Sanchez et al, 2020) and Junko (Ogawa, Iwata et al, 2020) described. Beyond that, more dramatic is the exclusive distribution of RfA1 particles in the cytoplasm, while spherical RfC droplets only existed in the nucleoplasm.…”

Section: Introductionsupporting

confidence: 73%

“…8c). On the other hand, reflectin proteins or reflectin variants described in this study make up a powerful arsenal to engineer human cells to achieve coloration, as Atrouli [20] and Junko [21] brilliant works have demonstrated.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, Daniel E. Morse and his team have preliminarily defined reflectin proteins as a new group of intrinsically disordered proteins (IDPs), and suggested that transient liquid-liquid phase separation (LLPS) may dominate reflectin assembly (Levenson et al, 2019). The dynamic reflectin assembly properties and the intricate reflectin-based biophotonic systems have already inspired the development of various next-generation tunable photonic (Dennis, Singh et al, 2017, Phan, Ordinario et al, 2015, Qin, Dennis et al, 2013 and electronic platforms and devices (Ordinario, Phan et al, 2014, Phan, Kautz et al, 2016, Yu, Li et al, 2014.…”

Section: Introductionmentioning

confidence: 99%

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Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins

Song

Liu

et al. 2021

Preprint

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Reflectins are membrane-bound proteins located in cephalopods iridocytes, with repeated canonical domains interspersed with cationic linkers. Scientists keep curious about their evolutionary processes, biochemical properties and intracellular functions. Here, by introducing reflectin A1, A2, B1 and C into HEK-293T cells, these proteins were found to phase out from the crowded intracellular milieu, with distinguished localization preferences. Inspired by their programmable block sequences, several truncated reflectin A1 (RfA1) peptides based on repetition of reflectin motifs were designed and transfected into cells. An obvious cyto-/nucleo-plasmic localization preference was once again observed. The dynamic performance of RfA1 derivatives and their analogic behavior between different reflectins suggest a conceivable evolutionary relationship among reflectin proteins. Additionally, a proteomic survey identified biochemical partners which contribute to the phase separation and intracellular localization of RfA1 and its truncations, as well as the close collaboration between RfA1 and the cytoskeleton systems. These findings indicate that liquid-liquid phase separation could be the fundamental mode for reflectins to achieve spatial organization, to cooperate with cytoskeleton during the regulation of reflective coloration. On the other hand, the dynamic behaviors of RfA1 derivatives strongly recommended themselves as programmable molecular tools.

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Section: Introductionsupporting

confidence: 73%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins

Song

Liu

et al. 2021

Preprint

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“…These proteins are effective controls to each other, with different self-assembly characteristics ( Levenson et al, 2016 ; Levenson et al, 2019 ) and membrane-bound properties ( Song et al, 2020 ). After transfection, reflectins are found to phase out from the crowded intracellular milieu, similar to what Atrouli ( Chatterjee et al, 2020 ) and Junko ( Ogawa et al, 2020 ) described. Beyond that, more dramatic is the exclusive distribution of RfA1 particles in the cytoplasm, while spherical RfC droplets only exist in the nucleoplasm.…”

Section: Introductionsupporting

confidence: 73%

“…Recently, two different groups made groundbreaking attempts and used reflectins to modify mammalian cell function. The formation of protein-based photonic architecture endows engineered human cells with tunable transparency-changing and light-scattering capabilities by expressing reflectins in the human embryonic kidney (HEK-293) cells ( Chatterjee et al, 2020 ; Ogawa et al, 2020 ). This is a milestone in the discovery of novel molecular tools to modify mammalian cells with new features ( Tang et al, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins

Song

Liu

et al. 2022

Front. Cell Dev. Biol.

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Reflectin proteins are natural copolymers consisting of repeated canonical domains. They are located in a biophotonic system called Bragg lamellae and manipulate the dynamic structural coloration of iridocytes. Their biological functions are intriguing, but the underlying mechanism is not fully understood. Reflectin A1, A2, B1, and C were found to present distinguished cyto-/nucleoplasmic localization preferences in the work. Comparable intracellular localization was reproduced by truncated reflectin variants, suggesting a conceivable evolutionary order among reflectin proteins. The size-dependent access of reflectin variants into the nucleus demonstrated a potential model of how reflectins get into Bragg lamellae. Moreover, RfA1 was found to extensively interact with the cytoskeleton, including its binding to actin and enrichment at the microtubule organizing center. This implied that the cytoskeleton system plays a fundamental role during the organization and transportation of reflectin proteins. The findings presented here provide evidence to get an in-depth insight into the evolutionary processes and working mechanisms of reflectins, as well as novel molecular tools to achieve tunable intracellular transportation.

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Engineering Hydrogel‐Based Biomedical Photonics: Design, Fabrication, and Applications

et al. 2021

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Light guiding and manipulation in photonics have become ubiquitous in events ranging from everyday communications to complex robotics and nanomedicine. The speed and sensitivity of light–matter interactions offer unprecedented advantages in biomedical optics, data transmission, photomedicine, and detection of multi‐scale phenomena. Recently, hydrogels have emerged as a promising candidate for interfacing photonics and bioengineering by combining their light‐guiding properties with live tissue compatibility in optical, chemical, physiological, and mechanical dimensions. Herein, the latest progress over hydrogel photonics and its applications in guidance and manipulation of light is reviewed. Physics of guiding light through hydrogels and living tissues, and existing technical challenges in translating these tools into biomedical settings are discussed. A comprehensive and thorough overview of materials, fabrication protocols, and design architectures used in hydrogel photonics is provided. Finally, recent examples of applying structures such as hydrogel optical fibers, living photonic constructs, and their use as light‐driven hydrogel robots, photomedicine tools, and organ‐on‐a‐chip models are described. By providing a critical and selective evaluation of the field's status, this work sets a foundation for the next generation of hydrogel photonic research.

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Genetic manipulation of the optical refractive index in living cells

Cited by 5 publications

References 14 publications

Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins

Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins

Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins

Engineering Hydrogel‐Based Biomedical Photonics: Design, Fabrication, and Applications

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