Record Display for the EPA National Library Catalog
RECORD NUMBER: 386 OF 416Main Title | The Plant Endoplasmic Reticulum [electronic resource] / | ||||
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Type | EBOOK | ||||
Author | Robinson, David G. | ||||
Publisher | Springer Berlin Heidelberg : Imprint: Springer, | ||||
Year Published | 2006 | ||||
Call Number | QH573-671 | ||||
ISBN | 9783540325321 | ||||
Subjects | Life sciences ; Cytology ; Plant anatomy ; Plant physiology | ||||
Internet Access |
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Collation | X, 338 p. online resource. | ||||
Notes | Due to license restrictions, this resource is available to EPA employees and authorized contractors only |
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Contents Notes | The Morphology and Dynamics of the ER -- Targeting of RNAs to ER Subdomains and its Relationship to Protein Localization -- The ER Folding Helpers: A Connection Between Protein Maturation, Stress Responses and Plant Development -- Endoplasmic Reticulum-associated Protein Degradation in Plant Cells -- ER-to-Golgi Transport: The COPII-Pathway -- Transport of Proteases to the Vacuole: ER Export Bypassing Golgi? -- Induction of Specialized Compartments from the ER -- Synthesis of Structural and Storage Lipids by the ER -- Oleosins and Endoplasmic Reticulum in Seeds and Anthers -- Participation of the Plant ER in Peroxisomal Biogenesis -- The ER and Plant Hormones -- The ER and Cell Calcium -- The ER Within Plasmodesmata -- The ER in Replication of Positive-Strand RNA Viruses. The endoplasmic reticulum (ER), called "the mother of all membranes," is spotlighted in this timely new book. The work presented here is especially exciting since GFP-technology has provided new ways of looking at the dynamics of the ER and its relationship to other organelles, particularly the Golgi apparatus and peroxisomes. This book provides in-depth knowledge of the ER and the diverse roles it plays-for instance, in protein trafficking, homeostasis of cellular calcium, plant hormone and lipid synthesis. These manifold activities are reflected in the great plasticity of the ER as a structure, with more than a dozen specialized domains recognized for this organelle. |