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10.1074/jbc.H118.002041 http://scihub22266oqcxt.onion/10.1074/jbc.H118.002041 C5868261!5868261!29572327     free     free     free       J+Biol+Chem 2018 ; 293 (12): 4575-6 Nephropedia Template TP {{tp|p=29572327|t=2018. A new actin-binding domain glues autophagy together |pdf=|usr=}}{{29572327}} gab.com Text A new actin-binding domain glues autophagy together JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=29572327 #FOAvip Autophagy breaks down nonessential cellular components to replenish macromolecular building blocks during starvation. Nevertheless, the downstream events regulating vesicle trafficking during this essential cellular process are not yet fully defined. Xu et al. combined approaches of crystallography, biochemistry, and cell biology to show that the guanine nucleotide exchange factor DENND3 contains an actin-binding site they call ?PHenn domain? in a region previously thought to be unstructured. PHenn domain binding to microfilaments is necessary for DENND3's participation in autophagy, providing a new link between autophagic stimulation and actin microfilaments. The findings by Xu et al. shed important new light on how membrane trafficking participates in critical steps of autophagy in relationship with actin microfilaments. Twit Text FOAVip A new actin-binding domain glues autophagy together ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=29572327 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29572327 #FOAvip English Wikipedia <ref>{{Cite pmid|29572327}}</ref> A new actin-binding domain glues autophagy together #MMPMID29572327 Wojnacki J; Galli T J Biol Chem 2018[Mar]; 293 (12): 4575-6 PMID29572327show ga Autophagy breaks down nonessential cellular components to replenish macromolecular building blocks during starvation. Nevertheless, the downstream events regulating vesicle trafficking during this essential cellular process are not yet fully defined. Xu et al. combined approaches of crystallography, biochemistry, and cell biology to show that the guanine nucleotide exchange factor DENND3 contains an actin-binding site they call ?PHenn domain? in a region previously thought to be unstructured. PHenn domain binding to microfilaments is necessary for DENND3's participation in autophagy, providing a new link between autophagic stimulation and actin microfilaments. The findings by Xu et al. shed important new light on how membrane trafficking participates in critical steps of autophagy in relationship with actin microfilaments. äA new actin-binding domain glues autophagy together (epmc).pdf DeepDyve Pubget Overpricing