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Microgels enable independent control of stiffness and interstitial space, overcoming limitations of conventional 3D hydrogels. Using fragmented gelatin methacryloyl microgels, we show that stiffness does not restrict non‐metastatic breast cancer growth, contrary to bulk hydrogels, and reveal the role of adherent‐to‐suspension transition in cancer ...
Danielle Vahala +15 more
wiley +1 more source
Boronic acid‐based fluorescent hybrids have been used as part of a versatile platform for real‐time metabolic bioimaging across cellular and organismal scales. Including glucose‐responsive imaging in living cells and in an insulin‐deficient vertebrate model, this work opens new opportunities for the development of precision diagnostics, metabolic ...
Haobo Ge +13 more
wiley +1 more source
Intrinsically stretchable OECTs enable bifunctional operations via gate engineering. Polarizable Ag/AgCl gates provide volatile sensing, while Au gates enable non‐volatile memory. The SEBS‐blended channel maintains performance under strain, supporting reliable signal transduction.
Jiyong Yoon +8 more
wiley +1 more source
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C2 Domains and Membrane Fusion
2011Publisher Summary This chapter describes C2 domains and membrane fusion. Membrane fusion or the controlled merger of two initially separated membranes is of fundamental importance in biology. This is particularly true for eukaryotic cells that contain a plethora of membrane-bound compartments.
Martens, Sascha, McMahon, Harvey T
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The C2 domains of synaptotagmin – partners in exocytosis
Trends in Biochemical Sciences, 2004Rapid signaling between neurons relies on the Ca(2+)-triggered exocytosis of neurotransmitters. Release is mediated by 'kiss-and-run' or complete fusion of secretory organelles with the plasma membrane. Current models indicate that exocytosis is regulated by synaptotagmin I (syt) and mediated by SNARE (soluble NSF-attachment protein receptor) proteins.
Jihong, Bai, Edwin R, Chapman
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Membrane binding and subcellular targeting of C2 domains
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2006C2 domains are a ubiquitous structural module and many of them function in Ca2+ -dependent membrane binding and thereby serve as Ca2+ effectors for divergent Ca2+ -mediated cellular processes. Extensive structural, biochemical, biophysical, and cellular studies of C2 domains and host proteins in the past decade have shown that due to their structural ...
Wonhwa, Cho, Robert V, Stahelin
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Science Signaling, 2001
The originally described C2 domains function as calcium-regulated phospholipid-binding domains. Several examples of proteins that have C2 domains (as identified by sequence similarity) have been found, yet these C2 domains have mutations in key residues that are required for calcium binding.
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The originally described C2 domains function as calcium-regulated phospholipid-binding domains. Several examples of proteins that have C2 domains (as identified by sequence similarity) have been found, yet these C2 domains have mutations in key residues that are required for calcium binding.
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Trends in Neurosciences, 2003
Abstract Ca 2+ influx into the presynaptic terminal triggers fusion of synaptic vesicles with the plasma membrane and release of neurotransmitters. A decade of intensive study of the synaptic vesicle protein synaptotagmin I has led to the general belief that this polypeptide functions as a Ca 2+ sensor in this process.
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Abstract Ca 2+ influx into the presynaptic terminal triggers fusion of synaptic vesicles with the plasma membrane and release of neurotransmitters. A decade of intensive study of the synaptic vesicle protein synaptotagmin I has led to the general belief that this polypeptide functions as a Ca 2+ sensor in this process.
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The Role of C2 Domains in PKC Signaling
2012More than two decades ago, the discovery of the first C2 domain in conventional Protein Kinase Cs (cPKCs) and of its role as a calcium-binding motif began to shed light on the activation mechanism of this family of Serine/Threonine kinases which are involved in several critical signal transduction pathways.
Carole A, Farah, Wayne S, Sossin
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Structure and mechanism of the unique C2 domain of Aida
The FEBS Journal, 2014Axin interactor, dorsalization‐associated (Aida) was identified as a regulatory factor that utilizes its C‐terminal region to interact with axis formation inhibitor (Axin). Aida abrogates the Axin‐mediated Jun N‐terminal kinase activation required for proper dorsalization during zebrafish embryonic development, and thus functions as a proventralization
Li-Sha, Zheng +10 more
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