• Cellular machinery for sensing mechanical force

    Hypothetical schematic model for mechanosensing mechanisms of various types of mechanosensors. (A) The cytoskeletal proteins linked to the actin cytoskeleton (F-actin) and adhesive structures that can undergo structural changes in response to mechanical force. The structural change can expose a binding site for other proteins to interact with, which can induce biochemical signaling. (B) Force acting on the ECM-tethered latency-associated peptide (LAP) by cells via integrin can induce a structural change in LAP. Due to the structural change, transforming growth factor (TGF) β can be released from the LAP complex. RGD; Arg-Gly-Asp (integrin binding site), ECM; extracellular matrix. (C) A stretchgated ion channel in Drosophila, NOMPC (no mechanoreceptor potential C), embedded in the membrane. Two of its four subunits are shown. S6 helices from each subunit block the passage of ions. These helices are linked to TRP domains that are captured by the cytoplasmic domains of the channel (left). The mechanical force that can stretch the cytoplasmic domain tethered to the microtubule can induce disposition of the TRP domains, which in turn induce structural changes in the S6 helices, leading to the opening of the channel (right). (D) The closed conformation of the TRAAK channel adopts a wedge shape, causing distortion of the lipid bilayer nearby (left). The open conformation of the channel adopts a cylinder shape (right). The projection areas of the cross-sections of the channel (yellow dotted lines) are shown in both the conformations. (E) Schematic illustrations of two subunits of Piezo1 are shown. Each of its three subunits has a curved conformation in the lipid bilayer, making a ‘dimple’ on the membrane (left). The central pore is suggested to be opened by tension in the lipid bilayer, which may flatten out the subunits (right).

BMB Reports 2018; 51(12): 609~665
Structural insights showing how arginine is able to be glycosylated by pathogenic effector proteins
Jun Bae Park, Youngki Yoo, and Hyun-Soo Cho
BMB Reports 2018; 51(12): 609-610  https://doi.org/10.5483/BMBRep.2018.51.12.269
A novel blood pressure modulator C1q/TNF-α–related protein 1 (CTRP1)
Sora Han, and Young Yang
BMB Reports 2018; 51(12): 611-612  https://doi.org/10.5483/BMBRep.2018.51.12.268
Invited Mini Reviews
Functions of DEAD box RNA helicases DDX5 and DDX17 in chromatin organization and transcriptional regulation
Guillaume Giraud, Sophie Terrone, and Cyril F. Bourgeois
BMB Reports 2018; 51(12): 613-622  https://doi.org/10.5483/BMBRep.2018.51.12.234
Cellular machinery for sensing mechanical force
Chul-Gyun Lim, Jiyoung Jang, and Chungho Kim
BMB Reports 2018; 51(12): 623-629  https://doi.org/10.5483/BMBRep.2018.51.12.237
Overexpression of CXCL2 inhibits cell proliferation and promotes apoptosis in hepatocellular carcinoma
Jun Ding, Kangdi Xu, Jie Zhang, Bingyi Lin, Yubo Wang, Shengyong Yin, Haiyang Xie, Lin Zhou, and Shusen Zheng
BMB Reports 2018; 51(12): 630-635  https://doi.org/10.5483/BMBRep.2018.51.12.140
Role of dipeptidyl peptidase-4 as a potentiator of activin/nodal signaling pathway
Dong-Seok Park, Kyuhee Kim, Minjoo Jang, and Sun-Cheol Choi
BMB Reports 2018; 51(12): 636-641  https://doi.org/10.5483/BMBRep.2018.51.12.210
UBE2S promotes the proliferation and survival of human lung adenocarcinoma cells
Zhi Liu, and Lijun Xu
BMB Reports 2018; 51(12): 642-647  https://doi.org/10.5483/BMBRep.2018.51.12.138
SPINK1 promotes cell growth and metastasis of lung adenocarcinoma and acts as a novel prognostic biomarker
Liyun Xu, Changchang Lu, Yanyan Huang, Jihang Zhou, Xincheng Wang, Chaowu Liu, Jun Chen, and Hanbo Le
BMB Reports 2018; 51(12): 648-653  https://doi.org/10.5483/BMBRep.2018.51.12.205
Tat-ATOX1 inhibits inflammatory responses via regulation of MAPK and NF-κB pathways
Dae Won Kim, Min Jea Shin, Yeon Joo Choi, Hyun Jung Kwon, Sung Ho Lee, Sunghou Lee, Jinseu Park, Kyu Hyung Han, Won Sik Eum, and Soo Young Choi
BMB Reports 2018; 51(12): 654-659  https://doi.org/10.5483/BMBRep.2018.51.12.248
HSP90 inhibitor, AUY922, debilitates intrinsic and acquired lapatinib-resistant HER2-positive gastric cancer cells
Kang-Seo Park, Yong Sang Hong, Junyoung Choi, Shinkyo Yoon, Jihoon Kang, Deokhoon Kim, Kang-Pa Lee, Hyeon-Su Im, Chang Hoon Lee, Seyoung Seo, Sang-We Kim, Dae Ho Lee, and Sook Ryun Park
BMB Reports 2018; 51(12): 660-665  https://doi.org/10.5483/BMBRep.2018.51.12.259


Current Issue

December 2018
Volume 51
Issue 12

2017 SCI Impact Factor 3.085


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