The Proline/Arginine-Rich Domain Is a Major Determinant of Dynamin Self-Activation

Barbara Barylko Lei Wang Derk D. Binns Justin A. Ross Tara C. Tassin Katie A. Collins David M. Jameson and Joseph P. Albanesi

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The Proline/Arginine-Rich Domain Is a Major Determinant of Dynamin Self-Activation

机译：脯氨酸/富含精氨酸的域是动力蛋白自我激活的主要决定因素

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Dynamins induce membrane vesiculation dur-ning endocytosis and Golgi budding in a process thatnrequires assembly-dependent GTPase activation. Brain-nspecific dynamin 1 has a weaker propensity to self-assemblenand self-activate than ubiquitously expressed dynamin 2.nHere we show that dynamin 3, which has important func-ntions in neuronal synapses, shares the self-assembly andnGTPase activation characteristics of dynamin 2. Analysisnof dynamin hybrids and of dynamin 1-dynamin 2 andndynamin 1-dynamin 3 heteropolymers reveals that concen-ntration-dependent GTPase activation is suppressed by thenC-terminal proline/arginine-rich domain of dynamin 1.nDynamin proline/arginine-rich domains also mediate inter-nactions with SH3 domain-containing proteins and thusnregulate both self-association and heteroassociation ofndynamins.

机译：动力蛋白在胞吞作用和高尔基体萌芽过程中诱导膜囊泡形成，该过程需要依赖组装的GTPase活化。脑非特异性动力蛋白1与普遍表达的动力蛋白2相比，具有较弱的自组装和自我激活倾向。n在此，我们证明了在神经元突触中具有重要功能的动力蛋白3具有与动力蛋白2相似的自组装和nGTPase活化特性。。对动力蛋白杂种以及动力蛋白1-dynamin 2和nddynamin 1- dynamin 3杂聚物的分析表明，浓度依赖性的GTPase活化被动力蛋白1的C末端脯氨酸/富含精氨酸的域所抑制，nDynamin脯氨酸/富含精氨酸的域也被抑制。介导与含SH3结构域的蛋白质的相互作用，从而同时调节地南宁的自缔合和异缔合。

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《Biochemistry》 |2010年第50期|p.10592-10594|共3页
作者
Barbara Barylko Lei Wang Derk D. Binns Justin A. Ross Tara C. Tassin Katie A. Collins David M. Jameson and Joseph P. Albanesi;
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‡Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas,Texas 75235-9041, United States, and §Department of Cell and Molecular Biology, John A. Burns School of Medicine,651 Ilalo Street, BSB 222, University of Hawaii, Honolulu, Hawaii 96813, United States;

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1. The Proline/Arginine-Rich Domain Is a Major Determinant of Dynamin Self-Activation [J] . Barylko B, Wang L, Binns DD, Biochemistry . 2010,第50期

机译：脯氨酸/富含精氨酸的域是动力蛋白自我激活的主要决定因素
2. Proline-rich domain in dynamin-2 has a low microtubule-binding activity: how is this activity controlled during mitosis in HeLa cells? [J] . Morita M, Hamao K, Izumi S, The Journal of Biochemistry . 2010,第5期

机译：dynamin-2中富含脯氨酸的结构域的微管结合活性较低：如何在HeLa细胞的有丝分裂过程中控制该活性？
3. Proline-rich domain in dynamin-2 has a low microtubule-binding activity: how is this activity controlled during mitosis in HeLa cells? [J] . Morita M, Hamao K, Izumi S, The Journal of Biochemistry . 2010,第5期

机译：dynamin-2中富含脯氨酸的结构域的微管结合活性较低：如何在HeLa细胞的有丝分裂过程中控制该活性？
4. The Application of Theory of Habitual Domains on English Majors' Extracurricular Reading [C] . Chen Tao, Zhao Caihong, Zhang Qing International Conference on Advances in Social Science, Humanities, and Management . 2013

机译：习惯域理论对英语专业课外阅读的应用
5. The role of targeting and effector domains in the functions of dynamin-family GTPases. [D] . King, Megan C. 2004

机译：靶向和效应子域在动力家族GTP酶的功能中的作用。
6. The Proline-Arginine Rich Domain (PRD) is a Major Determinant of Dynamin Self-Activation [O] . Barbara Barylko, Lei Wang, Derk D. Binns, -1

机译：脯氨酸精氨酸丰富的域（pRD）为动力素自激活的主要决定因素
7. Phosphatidylinositol (4,5)-Bisphosphate-dependent Activation of Dynamins I and II Lacking the Proline/Arginine-rich Domains [O] . Hsin Chieh Lin, Barbara Barylko, Mircea Achiriloaie, 1997

机译：磷脂酰肌醇（4,5） - 磷酸二磷酸依赖性动发电物I和II的活化缺乏脯氨酸/精氨酸富域

The Proline/Arginine-Rich Domain Is a Major Determinant of Dynamin Self-Activation

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