@article {1015,
	title = {Mechanochemical feedback control of dynamin independent endocytosis modulates membrane tension in adherent cells. [Microfluidics and Microfabrication Facility (INT)]},
	journal = {Nat Commun},
	volume = {9},
	year = {2018},
	month = {2018 10 11},
	pages = {4217},
	abstract = {<p>Plasma membrane tension regulates many key cellular processes. It is modulated by, and can modulate, membrane trafficking. However, the cellular pathway(s) involved in this interplay is poorly understood. Here we find that, among a number of endocytic processes operating simultaneously at the cell surface, a dynamin independent pathway, the CLIC/GEEC (CG) pathway, is rapidly and specifically upregulated upon a sudden reduction of tension. Moreover, inhibition (activation) of the CG pathway results in lower (higher) membrane tension. However, alteration in membrane tension does not directly modulate CG endocytosis. This requires vinculin, a mechano-transducer recruited to focal adhesion in adherent cells. Vinculin acts by controlling the levels of a key regulator of the CG pathway, GBF1, at the plasma membrane. Thus, the CG pathway directly regulates membrane tension and is in turn controlled via a mechano-chemical feedback inhibition, potentially leading to homeostatic regulation of membrane tension in adherent cells.</p>
},
	keywords = {Animals, Biomechanical Phenomena, Cell Adhesion, Cell Membrane, Dynamins, Endocytosis, Feedback, Physiological, Mechanotransduction, Cellular, Mice, Signal Transduction, Temperature, Vinculin},
	issn = {2041-1723},
	doi = {10.1038/s41467-018-06738-5},
	author = {Thottacherry, Joseph Jose and Kosmalska, Anita Joanna and Kumar, Amit and Vishen, Amit Singh and Elosegui-Artola, Alberto and Pradhan, Susav and Sharma, Sumit and Singh, Parvinder P and Guadamillas, Marta C and Chaudhary, Natasha and Vishwakarma, Ram and Trepat, Xavier and Del Pozo, Miguel A and Parton, Robert G and Rao, Madan and Pullarkat, Pramod and Roca-Cusachs, Pere and Mayor, Satyajit}
}
@article {519,
	title = {Unexpected histone H3 tail-clipping activity of glutamate dehydrogenase. (Mass spectrometry - Proteomics)},
	journal = {J Biol Chem},
	volume = {288},
	year = {2013},
	month = {2013 Jun 28},
	pages = {18743-57},
	abstract = {<p>Clipping of histone tails has been reported in several organisms. However, the significance and regulation of histone tail clipping largely remains unclear. According to recent discoveries H3 clipping has been found to be involved in regulation of gene expression and chromatin dynamics. Earlier we had provided evidence of tissue-specific proteolytic processing of histone H3 in White Leghorn chicken liver nuclei. In this study we identify a novel activity of glutamate dehydrogenase (GDH) as a histone H3-specific protease in chicken liver tissue. This protease activity is regulated by divalent ions and thiol-disulfide conversion in vitro. GDH specifically clips H3 in its free as well as chromatin-bound form. Furthermore, we have found an inhibitor that inhibits the H3-clipping activity of GDH. Like previously reported proteases, GDH too may have the potential to regulate/modulate post-translational modifications of histone H3 by removing the N-terminal residues of the histone. In short, our findings identify an unexpected proteolytic activity of GDH specific to histone H3 that is regulated by redox state, ionic concentrations, and a cellular inhibitor in vitro.</p>
},
	keywords = {Amino Acid Sequence, Animals, Binding Sites, Brain, Chickens, Chromatin, Cysteine Proteases, Disulfides, Epigenesis, Genetic, Gene Expression Regulation, Enzymologic, Glutamate Dehydrogenase, Histones, Hydrogen-Ion Concentration, Liver, Mass Spectrometry, Mice, Molecular Sequence Data, Rats, Recombinant Proteins, Salts, Sulfhydryl Compounds, Temperature},
	issn = {1083-351X},
	doi = {10.1074/jbc.M113.462531},
	author = {Mandal, Papita and Verma, Naveen and Chauhan, Sakshi and Tomar, Raghuvir S}
}
