Takashi Kanadome

ORCID: 0000-0002-8851-4780
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About
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Research Areas
  • Wnt/β-catenin signaling in development and cancer
  • Microtubule and mitosis dynamics
  • Endoplasmic Reticulum Stress and Disease
  • Cellular transport and secretion
  • Pancreatic function and diabetes
  • Ion channel regulation and function
  • S100 Proteins and Annexins
  • Axon Guidance and Neuronal Signaling
  • 14-3-3 protein interactions
  • Cellular Mechanics and Interactions
  • RNA Research and Splicing
  • Neuroscience and Neuropharmacology Research
  • Connexins and lens biology
  • Receptor Mechanisms and Signaling
  • Peroxisome Proliferator-Activated Receptors
  • Erythrocyte Function and Pathophysiology
  • Neurobiology and Insect Physiology Research
  • Protein Structure and Dynamics

Osaka University
2021-2024

Japan Science and Technology Agency
2021-2024

Osaka Research Institute of Industrial Science and Technology
2021

National Institute for Physiological Sciences
2019

National Institutes of Natural Sciences
2019

Nagoya University
2014-2016

Exit of cargo molecules from the endoplasmic reticulum (ER) for transport to Golgi is initial step in intracellular vesicular trafficking. The coat protein complex II (COPII) machinery recruited specialized regions ER, called ER exit sites (ERES), where it plays a central role early secretory pathway. It has been known more than two decades that calcium an essential factor vesicle trafficking apparatus. However, pathway complicated and poorly understood. We others previously identified...

10.1074/jbc.m114.592089 article EN cc-by Journal of Biological Chemistry 2014-12-25

Clustered protocadherin (Pcdh) functions as a cell recognition molecule through the homophilic interaction in central nervous system. However, its interactions have not yet been visualized neurons. We previously reported PcdhγB2-Förster resonance energy transfer (FRET) probes to be applicable only lines. Herein, we designed γB2-FRET by fusing FRET donor and acceptor fluorescent proteins single γB2 succeeded visualizing cultured hippocampal The probe localized soma neurites, signals, which...

10.1073/pnas.2301003120 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2023-09-11

Clustered protocadherin (Pcdh), a cell adhesion protein, is involved in the self-recognition and non-self-discrimination of neurons by conferring diversity on surface. Although roles Pcdh have been elucidated, it has challenging to visualize its activity neurons, which molecular function Pcdh. Here, we present fluorescent indicators, named IPADs, interaction protocadherin-α4 isoform (α4). IPADs successfully not only homophilic α4

10.1016/j.isci.2023.107238 article EN cc-by-nc-nd iScience 2023-07-01

Abstract N-cadherin (NCad) is a classical cadherin that mediates cell–cell interactions in Ca 2+ -dependent manner. NCad participates various biological processes, from ontogenesis to higher brain functions, though the visualization of living cells remains limited. Here, we present intensiometric interaction indicators, named INCIDERs, utilize dimerization-dependent fluorescent proteins. INCIDERs successfully visualize reversible across cells. Compared FRET-based have ~70-fold signal...

10.1038/s42003-022-04023-2 article EN cc-by Communications Biology 2022-10-07

Clustered protocadherins (Pcdhs), which are cell adhesion molecules, play a fundamental role in self-recognition and non-self-discrimination by conferring diversity on the surface. Although systematic cell-based aggregation assays provide information regarding binding properties of Pcdhs, direct visualization Pcdh trans interactions across cells remains challenging. Here, we present Förster resonance energy transfer (FRET)-based indicators for directly visualizing interactions. We developed...

10.1038/s41598-021-01481-2 article EN cc-by Scientific Reports 2021-11-15

cIPAD is a fluorescent indicator that allows the visualization of trans-interactions clustered protocadherin (Pcdh), cell adhesion molecule mediates neuronal self-recognition. We describe steps for using HEK293T cells to visualize Pcdh across as preliminary experiment before dissociated mouse neurons. then detail procedures visualizing between processes originating from same neurons, which are considered Pcdh-mediated For complete details on use and execution this protocol, please refer...

10.1016/j.xpro.2024.102844 article EN cc-by-nc-nd STAR Protocols 2024-01-25

Abstract Clustered protocadherin (Pcdh) functions as a cell recognition molecule through the homophilic interaction in CNS. However, its interactions have yet not been visualized neurons. We previously reported PcdhγB2-FRET probes to be applicable only for lines. Herein, we newly designed by fusing FRET donor and acceptor fluorescent proteins single PcdhγB2 succeeded visualizing cultured hippocampal The γB2-FRET probe localized soma neurites, signals were observed at contact sites between...

10.1101/2023.04.14.536980 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2023-04-15

Abstract Clustered protocadherins (Pcdhs), which are cell adhesion molecules, play a fundamental role in self-recognition and non-self-discrimination by conferring diversity on the surface. Although systematic cell-based aggregation assays provide information regarding binding properties of Pcdhs, direct visualization Pcdh trans interactions across cells remains challenging. Here, we present Förster resonance energy transfer (FRET)-based indicators for directly visualizing interactions. We...

10.21203/rs.3.rs-841788/v1 preprint EN cc-by Research Square (Research Square) 2021-09-01
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