caa a22 4500 445840145 CHVBK 20180317145341.0 cr unu---uuuuu 170323e20110101xx s 000 0 eng 10.1007/s00709-010-0247-0 doi (NATIONALLICENCE)springer-10.1007/s00709-010-0247-0 Biology of callose (β-1,3-glucan) turnover at plasmodesmata [Elektronische Daten] [Raul Zavaliev, Shoko Ueki, Bernard Epel, Vitaly Citovsky] The turnover of callose (β-1,3-glucan) within cell walls is an essential process affecting many developmental, physiological and stress related processes in plants. The deposition and degradation of callose at the neck region of plasmodesmata (Pd) is one of the cellular control mechanisms regulating Pd permeability during both abiotic and biotic stresses. Callose accumulation at Pd is controlled by callose synthases (CalS; EC 2.4.1.34), endogenous enzymes mediating callose synthesis, and by β-1,3-glucanases (BG; EC 3.2.1.39), hydrolytic enzymes which specifically degrade callose. Transcriptional and posttranslational regulation of some CalSs and BGs are strongly controlled by stress signaling, such as that resulting from pathogen invasion. We review the role of Pd-associated callose in the regulation of intercellular communication during developmental, physiological, and stress response processes. Special emphasis is placed on the involvement of Pd-callose in viral pathogenicity. Callose accumulation at Pd restricts virus movement in both compatible and incompatible interactions, while its degradation promotes pathogen spread. Hence, studies on mechanisms of callose turnover at Pd during viral cell-to-cell spread are of importance for our understanding of host mechanisms exploited by viruses in order to successfully spread within the infected plant. Springer-Verlag, 2010 Plasmodesmata nationallicence Callose nationallicence β-1,3-Glucanase nationallicence Callose synthase nationallicence Pathogenesis-related proteins nationallicence Virus spread nationallicence BG : β-1,3-glucanase nationallicence β-1,3-glucan hydrolase nationallicence CalS : Callose synthase nationallicence ER : Endoplasmic reticulum nationallicence GSL : Glucan synthase-like nationallicence MP : Movement protein nationallicence Pd : Plasmodesmata nationallicence PR : Pathogenesis related nationallicence SAR : Systemic acquired resistance nationallicence SEL : Size exclusion limit nationallicence Zavaliev Raul Department of Molecular Biology and Ecology of Plants, Tel Aviv University, 69978, Tel Aviv, Israel aut Ueki Shoko Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, 11794-5215, Stony Brook, NY, USA aut Epel Bernard Department of Molecular Biology and Ecology of Plants, Tel Aviv University, 69978, Tel Aviv, Israel aut Citovsky Vitaly Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, 11794-5215, Stony Brook, NY, USA aut Protoplasma Springer Vienna 248/1(2011-01-01), 117-130 0033-183X 248:1<117 2011 248 709 https://doi.org/10.1007/s00709-010-0247-0 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00709-010-0247-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Zavaliev Raul Department of Molecular Biology and Ecology of Plants, Tel Aviv University, 69978, Tel Aviv, Israel aut NATIONALLICENCE 700 1- Ueki Shoko Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, 11794-5215, Stony Brook, NY, USA aut NATIONALLICENCE 700 1- Epel Bernard Department of Molecular Biology and Ecology of Plants, Tel Aviv University, 69978, Tel Aviv, Israel aut NATIONALLICENCE 700 1- Citovsky Vitaly Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, 11794-5215, Stony Brook, NY, USA aut NATIONALLICENCE 773 0- Protoplasma Springer Vienna 248/1(2011-01-01), 117-130 0033-183X 248:1<117 2011 248 709 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer