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Faisal Inayat,Aysha Aslam,Mathew D. Grunwald,Qulsoom Hussain,Abu Hurairah,Shahzad Iqbal 대한소화기내시경학회 2019 Clinical Endoscopy Vol.52 No.3
Gastrointestinal stromal tumors (GISTs) are the most common mesenchymal tumors of the gastrointestinal tract, primarily arisingfrom the stomach. With the widespread utilization of and technical advancements in endoscopy, gastric GISTs are being increasinglydetected at an early stage, enabling complete endoscopic resection. Endoscopic full-thickness resection (EFTR) is an advancedtechnique that has been recognized as a treatment tool for neoplasms in the digestive tract in selected patients. Although a numberof methods are available, closing large iatrogenic defects after EFTR can be a concern in clinical practice. If this potential problem isappropriately solved, patients with gastric GISTs would be suitable candidates for resection utilizing this technique. To our knowledge,this is the first study to propose omental patching and purse-string endosuture closure following EFTR as a feasible endoscopic optionin patients with gastric GISTs.
ULK1 phosphorylates Ser30 of BECN1 in association with ATG14 to stimulate autophagy induction
Park, Ji-Man,Seo, Minchul,Jung, Chang Hwa,Grunwald, Douglas,Stone, Matthew,Otto, Neil Michael,Toso, Erik,Ahn, Yeseul,Kyba, Michael,Griffin, Timothy J.,Higgins, LeeAnn,Kim, Do-Hyung Informa UK (TaylorFrancis) 2018 AUTOPHAGY Vol.14 No.4
<P>ULK1 (unc51-like autophagy activating kinase 1) is a serine/threonine kinase that plays a key role in regulating macroautophagy/autophagy induction in response to amino acid starvation. Despite the recent progress in understanding ULK1 functions, the molecular mechanism by which ULK1 regulates the induction of autophagy remains elusive. In this study, we determined that ULK1 phosphorylates Ser30 of BECN1 (Beclin 1) in association with ATG14 (autophagy-related 14) but not with UVRAG (UV radiation resistance associated). The Ser30 phosphorylation was induced by deprivation of amino acids or treatments with Torin 1 or rapamycin, the conditions that inhibit MTORC1 (mechanistic target of rapamycin complex 1), and requires ATG13 and RB1CC1 (RB1 inducible coiled-coil 1), proteins that interact with ULK1. Hypoxia or glutamine deprivation, which inhibit MTORC1, was also able to increase the phosphorylation in a manner dependent upon ULK1 and ULK2. Blocking the BECN1 phosphorylation by replacing Ser30 with alanine suppressed the amino acid starvation-induced activation of the ATG14-containing PIK3C3/VPS34 (phosphatidylinositol 3-kinase catalytic subunit type 3) kinase, and reduced autophagy flux and the formation of phagophores and autophagosomes. The Ser30-to-Ala mutation did not affect the ULK1-mediated phosphorylations of BECN1 Ser15 or ATG14 Ser29, indicating that the BECN1 Ser30 phosphorylation might regulate autophagy independently of those 2 sites. Taken together, these results demonstrate that BECN1 Ser30 is a ULK1 target site whose phosphorylation activates the ATG14-containing PIK3C3 complex and stimulates autophagosome formation in response to amino acid starvation, hypoxia, and MTORC1 inhibition.</P>