
@article {166929,
	title = {Syntaxin11 Deficiency Inhibits CRAC Channel Priming to Suppress Cytotoxicity and Gene Expression in T Lymphocytes},
	journal = {eLife},
	year = {2026},
	month = {May 22, 2026},
	abstract = {<p class="rtejustify">Mutations in Syntaxin11, a Q-SNARE, result in a fatal immune disorder known as familial hemophagocytic lymphohistiocytosis 4 (FHLH4) in human patients. A key diagnostic feature of FHLH4 is defective T and natural killer (NK) cell cytotoxicity. Here we show that Syntaxin11 directly binds and regulates Orai1, the pore forming subunit of calcium release activated calcium (CRAC) channels. CRAC channels enable store-operated calcium entry (SOCE) from the extracellular space and are crucial for granule exocytosis and nuclear factor of activated T cells (NFAT) dependent gene expression in activated lymphocytes. Syntaxin11 depletion strongly inhibited SOCE, CRAC currents, NFAT activation, interleukin-2 gene expression and degranulation in FHLH4 patient T lymphocytes and cell lines. Remarkably, defects of granule exocytosis as well as interleukin-2 expression could be reversed by ionomycin in patient T lymphocytes and a constitutively active, H134S, mutant of Orai1 rescued calcium entry in Syntaxin11 depleted cells. Further analyses showed that Syntaxin11 primes Orai1 for optimal on-site multimeric assembly which was Stim independent but required for gating. Priming of ion channel pore subunits is, therefore, a primary function of specific SNAREs which may have preceded their role in vesicle fusion.</p>
},
	doi = {10.7554/elife.111335.1},
	url = {http://dx.doi.org/10.7554/eLife.111335.1},
	author = {Datta, Sritama and Gupta, Abhikarsh and Jagetiya, Kunal Mukesh and Bera, Resmi and Tiwari, Vikas and Yande, Atharva Rahul and Yamashita, Megumi and Rishad, Abdul and Malik, Vishal and Raran-Kurussi, Sreejith and Ammann, Sandra and Shahrooei, Mohammad and Mandal, Kalyaneswar and Sowdhamini, Ramanathan and Prakriya, Murali and Dani, Adish and Vig, Monika}
}
@article {102046,
	title = {Rational Design of Protein-Specific Folding Modifiers.},
	journal = {J Am Chem Soc},
	year = {2021},
	month = {2021 Nov 01},
	abstract = {<p>Protein-folding can go wrong and , with significant consequences for the living organism and the pharmaceutical industry, respectively. Here we propose a design principle for small-peptide-based protein-specific folding modifiers. The principle is based on constructing a "xenonucleus", which is a prefolded peptide that mimics the folding nucleus of a protein. Using stopped-flow kinetics, NMR spectroscopy, F{\"o}rster resonance energy transfer, single-molecule force measurements, and molecular dynamics simulations, we demonstrate that a xenonucleus can make the refolding of ubiquitin faster by 33 {\textpm} 5\%, while variants of the same peptide have little or no effect. Our approach provides a novel method for constructing specific, genetically encodable folding catalysts for suitable proteins that have a well-defined contiguous folding nucleus.</p>
},
	issn = {1520-5126},
	doi = {10.1021/jacs.1c09611},
	author = {Das, Anirban and Yadav, Anju and Gupta, Mona and R, Purushotham and Terse, Vishram L and Vishvakarma, Vicky and Singh, Sameer and Nandi, Tathagata and Banerjee, Arkadeep and Mandal, Kalyaneswar and Gosavi, Shachi and Das, Ranabir and Ainavarapu, Sri Rama Koti and Maiti, Sudipta}
}
