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      Functional Mechanism of Calmodulin for Cellular Responses in Plants

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      https://www.riss.kr/link?id=A76310091

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      국문 초록 (Abstract)

      Ca2?은 다양한 자극과 빛, biotic, abiotic 스트레스, 호르몬 등의 반응에 대한 세포내 2차 신호전달물질로써 중요한 역할을 한다. Ca2?의 반응자들은 특정 물질과 경로를 활성화함으로써 신호전달 기능을 한다고 알려져 있는 Ca2?결합 단백질들이다. 이들 단백질 중, calmidulin (CaM)은 식물과 동물의 특정 단백질의 활성을 조절하는 것으로 잘 알려져 왔다. 특히, 식물은 다양한 CaM 유전자와 특징적인 protein kinase와 전사인자를 포함한 많은 종류의 CaM관련 단백질들을 가지고 있다. 이로 인해서 식물은 주변의 여러 가지 신호들을 인지할 수 있을 뿐만 아니라 변화된 환경에 적응할 수 있는 것이다. 하지만, 대부분의 CaM이나 이들과 관련된 단백질들의 기능은 최근 활발히 연구되고 있지만 아직 많은 작용 기작이 연구의 대상이 되고 있다. 따라서 CaM의 기능을 좀 더 이해한다면 식물의 환경적 자극에 대한 반응과 식물의 성장과 발달에 있어서 CaM의 역할을 규명하는데 도움을 줄 수 있을 것으로 기대된다. 본 논문은 Ca2?-CaM의 신호전달 시스템과, CaM과 관련된 단백질들, 그리고 식물의 biotic, abiotic 스트레스에 대한 외부 자극의 반응에 있어서 CaM의 작용에 대해 기술하였다.
      번역하기

      Ca2?은 다양한 자극과 빛, biotic, abiotic 스트레스, 호르몬 등의 반응에 대한 세포내 2차 신호전달물질로써 중요한 역할을 한다. Ca2?의 반응자들은 특정 물질과 경로를 활성화함으로써 신호전달 ...

      Ca2?은 다양한 자극과 빛, biotic, abiotic 스트레스, 호르몬 등의 반응에 대한 세포내 2차 신호전달물질로써 중요한 역할을 한다. Ca2?의 반응자들은 특정 물질과 경로를 활성화함으로써 신호전달 기능을 한다고 알려져 있는 Ca2?결합 단백질들이다. 이들 단백질 중, calmidulin (CaM)은 식물과 동물의 특정 단백질의 활성을 조절하는 것으로 잘 알려져 왔다. 특히, 식물은 다양한 CaM 유전자와 특징적인 protein kinase와 전사인자를 포함한 많은 종류의 CaM관련 단백질들을 가지고 있다. 이로 인해서 식물은 주변의 여러 가지 신호들을 인지할 수 있을 뿐만 아니라 변화된 환경에 적응할 수 있는 것이다. 하지만, 대부분의 CaM이나 이들과 관련된 단백질들의 기능은 최근 활발히 연구되고 있지만 아직 많은 작용 기작이 연구의 대상이 되고 있다. 따라서 CaM의 기능을 좀 더 이해한다면 식물의 환경적 자극에 대한 반응과 식물의 성장과 발달에 있어서 CaM의 역할을 규명하는데 도움을 줄 수 있을 것으로 기대된다. 본 논문은 Ca2?-CaM의 신호전달 시스템과, CaM과 관련된 단백질들, 그리고 식물의 biotic, abiotic 스트레스에 대한 외부 자극의 반응에 있어서 CaM의 작용에 대해 기술하였다.

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      다국어 초록 (Multilingual Abstract)

      Calcium (Ca2?) plays pivotal roles as an intracellular second messenger in response to a variety of stimuli, including light, abiotic- and biotic stresses and hormones. Ca2? sensor is Ca2?-binding protein known to function in transducing signals by activating specific targets and pathways. Among Ca2?-binding proteins, calmodulin (CaM) has been well reported to regulate the activity of downstream target proteins in plants and animals. Especially plants possess multiple CaM genes and many CaM target proteins, including unique protein kinases and transcription factors. Thus, plants are possible to perceive different signals from their surroundings and adapt to the changing environment. However, the function of most of CaM or CaM-related proteins have been remained uncharacterized and unknown. Hence, a better understanding of the function of these proteins will help in deciphering their roles in plant growth, development and response to environmental stimuli. This review focuses on Ca2?-CaM messenger system, CaM-associated proteins and their role in responses to external stimuli of both abiotic and biotic stresses in plants.
      번역하기

      Calcium (Ca2?) plays pivotal roles as an intracellular second messenger in response to a variety of stimuli, including light, abiotic- and biotic stresses and hormones. Ca2? sensor is Ca2?-binding protein known to function in transducing signals by ac...

      Calcium (Ca2?) plays pivotal roles as an intracellular second messenger in response to a variety of stimuli, including light, abiotic- and biotic stresses and hormones. Ca2? sensor is Ca2?-binding protein known to function in transducing signals by activating specific targets and pathways. Among Ca2?-binding proteins, calmodulin (CaM) has been well reported to regulate the activity of downstream target proteins in plants and animals. Especially plants possess multiple CaM genes and many CaM target proteins, including unique protein kinases and transcription factors. Thus, plants are possible to perceive different signals from their surroundings and adapt to the changing environment. However, the function of most of CaM or CaM-related proteins have been remained uncharacterized and unknown. Hence, a better understanding of the function of these proteins will help in deciphering their roles in plant growth, development and response to environmental stimuli. This review focuses on Ca2?-CaM messenger system, CaM-associated proteins and their role in responses to external stimuli of both abiotic and biotic stresses in plants.

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      목차 (Table of Contents)

      • Introduction
      • CaM binding proteins
      • CaM in plant responses to biotic and abiotic signals
      • Future studies
      • References
      • Introduction
      • CaM binding proteins
      • CaM in plant responses to biotic and abiotic signals
      • Future studies
      • References
      • 초록
      더보기

      참고문헌 (Reference)

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      1 Arazi, T., "tobacco plasma membrane calmodulin-binding transporter confers Ni2+ tolerance and Pb2+ hypersensitivity in transgenic plants" 20 : 171-182, 1999

      2 Harding, S. A., "Transgenic tobacco expressing a foreign calmodulin gene shows an enhanced production of active oxygen species" 16 : 1137-1144, 1997

      3 Knight, M. R., "Transgenic plant aequorin reports the effects of touch and cold-shock and elicitors on cytoplasmic calcium" 352 : 524-526, 1991

      4 Locy, R. D., "The regulation of GABA accumulation by heat stress in Arabidopsis in Plant tolerance to abiotic stresses in agriculture: role of genetic engineering" Kluwer Academic Publishers 39-53, 2000

      5 Benjamins, R., "The PINOID protein kinase regulates organ development in Arabidopsis by enhancing polar auxin transport" 128 : 4057-4067, 2001

      6 Clough, S. J., "The Arabidopsis dnd1 ‘defense, no death’ gene encodes a mutated cyclic nucleotide-gated ion channel" 97 : 9323-9328, 2000

      7 Ryals, J. A., "Systemic acquired resistance" 8 : 1809-1819, 1996

      8 Desikan, R. A. -H., "Regulation of the Arabidopsis transcriptome by oxidative stress" 127 : 159-172, 2001

      9 Hsieh, H. L., "Regulation of a recombinant pea nuclear apyrase by CaM and casein kinase II" 1494 : 248-255, 2000

      10 Cho, M. J., "Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms" 37 : 15593-15597, 1998

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      27 Reddy, A. S. N., "Isolation and characterization of a novel calmodulin-binding protein from potato" 277 : 4206-4214, 2002

      28 Heo, W. D., "Involvement of specific calmodulin isoforms in salicylic acid-independent activation of plant disease resistance responses" 96 : 766-771, 1999

      29 Aurisano, N., "Involvement of calcium and calmodulin in protein and amino acids metabolism in rice roots under anoxia" 36 : 1525-1529, 1995

      30 Yoo, B. C., "Intramolecular binding contributes to the activation of CDPK, a protein kinase with a calmodulin-like domain" 35 : 12029-12037, 1996

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      32 Chung, W. S., "Identification of a calmodulin- regulated soybean Ca2+-ATPase (SCA1) that is located in the plasma membrane" 12 : 1393-1408, 2000

      33 Yang, T., "Hydrogen peroxide homeostasis: activation of plant catalase by calcium/ calmodulin" 99 : 4097-4102, 2002

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      39 Chen, Y. L., "Extracellular calmodulin-induced stomatal closure is mediated by heterotrimeric G protein and H2O2" 136 : 4096-4103, 2004

      40 Sunkar, R., "Expression of a truncated tobacco NtCBP4 channel in transgenic plants and disruption of the homologous Arabidopsis CNGC1 gene confer Pb2+ tolerance" 24 : 533-542, 2000

      41 Goldstein,G.W., "Evidence that lead acts as a calcium substitute in second messenger metabolism" 14 : 97-101, 1993

      42 McAinsh, M., "Encoding specificity in Ca2+ signalling systems" 3 : 32-36, 1998

      43 Leng, Q., "Electrophysiological analysis of cloned cyclic nucleotide-gated ion channels" 128 : 400-410, 2002

      44 Jones, D. L., "Effect of aluminum on cytoplasmic Ca2+ homeostasis in root hairs of Arabidopsis thaliana (L.)" 206 : 378-387, 1998

      45 Takezawa, D., "Dual regulation of a chimeric plant serine/threonine kinase by calcium and calcium/ calmodulin" 271 : 8126-8132, 1996

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      47 Steinebrunner, I., "Disruption of apyrases inhibits pollen germination in Arabidopsis" 131 : 1638-1647, 2003

      48 Lee, S. H., "Differential regulation of Ca2+/calmodulin-dependent enzymes by plant calmodulin isoforms and free Ca2+ concentration" 350 : 299-306, 2000

      49 Kuriu, T., "Defect of cold sensitive response in calmodulin mutants of Paramecium and the restoration by cyclic nucleotide" 22 : 493-500, 1997

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      55 Patil, S., "Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain" 92 : 4897-4901, 1995

      56 Dash, S., "Characterization of the basic amphiphilic α-helix calmodulin-binding domain of a 61.5 kDa tobacco calmodulin-binding protein" 36 : 2025-2029, 1997

      57 Kohler, C., "Characterization of calmodulin binding to cyclic nucleotide-gated ion channels from Arabidopsis thaliana" 471 : 133-136, 2000

      58 Luan, S., "Calmodulins and calcineurin B-like proteins: calcium sensors for specific signal response coupling in plants" 14 : 389-400, 2002

      59 Snedden, W. A., "Calmodulin, calmodulin-related proteins and plant responses to the environment" 3 : 299-304, 1998

      60 Kim, M. C., "Calmodulin interacts with MLO protein to regulate defence against mildew in barley" 416 : 447-451, 2002

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      81 Arazi, T., "A high affinity calmodulin-binding site in a tobacco plasma-membrane channel protein coincides with a characteristic element of cyclic nucleotide-binding domains" 42 : 591-601, 2000

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      84 Reddy, A. S. N., "A calmodulin binding protein from Arabidopsis is induced by ethylene and contains a DNA-binding motif" 279 : 762-769, 2000

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      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2027 평가예정 재인증평가 신청대상 (재인증)
      2021-01-01 평가 등재학술지 유지 (재인증) KCI등재
      2018-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2015-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2011-08-03 학술지명변경 외국어명 : Korean Journal of Life Science -> Journal of Life Science KCI등재
      2011-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2009-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2007-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2004-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      2003-01-01 평가 등재후보 1차 PASS (등재후보1차) KCI등재후보
      2001-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      학술지 인용정보

      학술지 인용정보
      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 0.37 0.37 0.42
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.43 0.43 0.774 0.09
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