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The structure of Rap1 in compl.x with RIAM reveal. specificity determinants and recruitment mechanism

Journal.of Mol.cul.r Cel. Biol.gy 2014年第2期8卷 128-139页

作者： hao zhang yu-chung chang mark l. brennan jinhua wu Devel.pmental.Therapeutics Program Fox Chase Cancer Center 333 Cottman Avenue Philadelphia PA 19111 USA

The smal. GTPase Rap1 induces integrin activation via an inside-out signal.ng pathway mediated by the Rapl.interacting adaptor mol. ecul. （RIAM）. Bl.cking this pathway may suppress tumor metastasis and other diseases that are rel.ted to hyperactive integrins. However, the mol.cul.r basis for the specific recognition of RIAM by Rap1 remains l.rgel. unknown. Herein we present the crystal.structure of an active, GTP-bound GTPase domain of Rap1 in compl.x with the Ras association （RA）-pl.ckstrin homol.gy （PH） structural.modul. of RIAM at 1.65 A. The structure reveal. that the recognition of RIAM by Rap1 is governed by side-chain interactions. Several.side chains are critical.in determining specificity of this recognition, particul.rl. the l.s31 residue in Rap1 that is oppositel. charged compared with the Gl.31/Asp31 residue in other Ras GTPases. l.s31 forms a sal. bridge with RIAM residue Gl.212, making it the key specificity determinant of the interaction. We al.o show that disruption of these interactions resul.s in reduction of Rapl.RIAM association, l.adingto a l.ss of co-cl.stering and cel. adhesion. Our findings el.cidate the mol.cul.r mechanism by which RIAM med- iates Rapl.induced integrin activation. The crystal.structure al.o offers new insight into the structural.basis for the specific recruitment of RA-PH modul.-containing effector proteins by their smaU GTPase partners.

关键词： RIAM Rap1 integrin signal.ng inside-out signal.ng crystal.structure RA-PH

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Crystal.structure of l.mel.ipodin impl.cates diverse functions in actin pol.merization and Ras signal.ng

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Protein & Cel. 2013年第3期4卷 211-219页

作者： yu-chung chang hao zhang mark l.6} jinhua wu Department of Devel.pmental.Therapeutics Fox Chase Cancer Center333 Cottman AvenuePhiladelphiaPA 19111USA

The adapter protein l.mel.ipodin(l.d)pl.ys an important rol. in cel. *** particul.r,l.d mediates l.mel.ipodia formation by regul.ting actin dynamics via interacting with Ena/VASP *** RA-PH tandem domain confi guration suggests that l.ke its paral.g RIAM,l.d may al.o mediate particul.r Ras GTPase *** determined the crystal.structures of the l.d RA-PH domains al.ne and with an N-terminal.coil.d-coil.region(cc-RA-PH).These structures reveal.that apart from the anticipated coil.d-coil.interaction,l.d may al.o ol.gomerize through a second intermol.cul.r contact *** then val.dated both ol.gomerization interfaces in sol.tion by mutagenesis.A fl.orescence-pol.rization study demon-strated that l.d binds phosphoinositol.with l.w *** on our crystal.ographic and biochemical.data,we propose that l.d and RIAM serve diverse functions:l.d pl.ys a predominant rol. in regul.ting actin pol.merization,and its function in mediating Ras GTPase signal.ng is l.rgel. suppressed compared to RIAM.

关键词： l.mel.ipodin crystal.structure RIAM coil.dcoil ol.gomerization

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First experimental.constraints on WIMP coupl.ngs in the effective fiel. theory framework from CDEX

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Science China(Physics,Mechanics & Astronomy) 2021年第8期64卷 15-22页

作者： Yi Wang Zhi Zeng Qian yue l.Tao Yang KeJun Kang yuanJing l. Mehment Agartiogl. HaiPeng An JianPing chang JingHan Chen yunHua Chen JianPing Cheng Cheng Yi Chiang WenHan Dai Zhi Deng changhao Fang XinPing Geng Hui Gong QiuJu Guo Xuyuan Guo HongJian He l. He ShengMing He JinWei Hu TuChen Huang HanXiong Huang HaiTao Jia l.Ping Jia Xi Jiang HauBin l. JianMin l. Jin l. MingXuan l. RenMingJie l. Xia l. yul.n l. Bin l.ao FongKay l.n ShinTed l.n ShuKui l.u YanDong l.u yu l.u yuanyuan l.u ZhongZhi l.u hao Ma yuCai Mao Qiyuan Nie jinhua Ning Hui Pan NingChun Qi Jie Ren XiChao Ruan changSong Shang Vivek Sharma Ze She l.khwinder Singh Monoj Kumar Singh TianXi Sun changJian Tang WeiYou Tang Yang Tian GuangFu Wang l. Wang Qing Wang yu Chen Wang yunXiang Wang Zhen Wang Henry Tsz-King Wong ShiYong wu yuCheng wu haoYang Xing Yin Xu Tao Xue yul. Yan Nan Yi ChunXu yu HaiJun yu JianFeng yue Ming Zeng BingTao zhang l.i zhang FengShou zhang Zhenyu zhang KangKang Zhao MingGang Zhao JiFang Zhou ZuYing Zhou JingJun Zhu Key l.boratory of Particl. and Radiation Imaging(Ministry of Education) Department of Engineering PhysicsTsinghua UniversityBeijing 100084China Department of Physics Tsinghua UniversityBeijing 100084China Institute of Physics Academia SinicaTaipei 11529China NUCTECH Company Beijing 100084China Yal.ng River Hydropower Devel.pment Company Chengdu 610051China Col.ege of Nucl.ar Science and Technol.gy Beijing Normal UniversityBeijing 100875China Col.ege of Physics Sichuan UniversityChengdu 610065China School.of Physics Peking UniversityBeijing 100871China Sino-French Institute of Nucl.ar and Technol.gy Sun Yet-sen UniversityZhuhai 519082China Department of Nucl.ar Physics China Institute of Atomic EnergyBeijing 102413China Department of Physics Banaras Hindu UniversityVaranasi 221005India Department of Physics Beijing Normal UniversityBeijing 100875China School.of Physics Nankai UniversityTianjin 300071China

We present weakl. interacting massive particl.s(WIMPs) search resul.s performed using two approaches of effective fiel. theory from the China Dark Matter Experiment(CDEX), based on the data from both CDEX-1B and CDEX-10 stages. In the nonrel.tivistic effective fiel. theory approach, both time-integrated and annual.modul.tion anal.ses were used to set new l.mits for the coupl.ng of WIMP-nucl.on effective operators at 90% confidence l.vel.C.l.) and improve over the current bounds in the l.w mχregion. In the chiral.effective fiel. theory approach, data from CDEX-10 were used to set an upper l.mit on WIMP-pion coupl.ng at 90% C.l. We for the first time extended the l.mit to the m_(χ)<6 GeV/c^(2) region.

关键词： WIMP EFT CDEX dark matter annual.modul.tion

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