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International review of cell and molecular biology. Volume 292 [electronic resource] / edited by Kwang W. Jeon

Published:
Waltham, MA : Elsevier Academic Press, 2011.
Physical Description:
1 online resource (208 pages)
Additional Creators:
Jeon, Kwang W.
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Contents:
Machine generated contents note: ch. One New Insights into the Mechanisms of Cytomotive Actin and Tubulin Filaments / Linda A. Amos -- 1.Introduction -- 2.Mechanisms of Directed Movement -- 2.1.Treadmilling -- 2.2.Dynamic instability -- 2.3.Choice of mechanism is determined by subtle differences -- 2.4.Membrane shaping and remodeling -- 3.The Tubulin/FtsZ Family -- 3.1.Evolutionary gap in living organisms -- 3.2.Filaments and tubes -- 3.3.Conformational changes in protofilaments -- 3.4.Atomic structures of tubulin family -- 3.5.Assembly and the nucleotide hydrolysis cycle -- 3.6.New insights from TubZ filaments -- 3.7.Lateral interactions in the tubulin family -- 3.8.Roles of the C-termini -- 3.9.Tubulin-binding drugs -- 3.10.EB proteins -- 3.11.So, what is the initial state of GTP-bound protofilaments? -- 3.12.Control of microtubule dynamics by accessory proteins -- 3.13.γ-Tubulin complexes -- 3.14.Less well-known tubulin family members -- 3.15.Microtubules are flexible in spite of being stiff -- 4.The Actin Family -- 4.1.Actin family filament complexes -- 4.2.Atomic structures of the actin family -- 4.3.Nucleotide hydrolysis -- 4.4.Lateral interactions in actin filaments -- 4.5.Filament dynamics in the actin family -- 5.Concluding Remarks and Future Directions -- 5.1.Conformational changes associated with nucleotide hydrolysis cycles -- 5.2.Subunit conformations at filament ends -- 5.3.Cooperativity -- 5.4.Relationships between family members help trace the course of evolution -- Acknowledgments -- References -- ch. Two New Insights into the Role of Mitochondria-Associated Endoplasmic Reticulum Membrane / Teruo Hayashi -- 1.Introduction -- 2.Structural and Functional Heterogeneity of the ER -- 3.The Structure of the MAM -- 3.1.Origin and formation of the MAM -- 3.2.Dynamics of the MAM-mitochondria complex -- 3.3.Visualization of the MAM -- 3.4.Purification of the MAM -- 4.Components of the MAM -- 4.1.Protein components of the MAM -- 4.2.Lipid components of the MAM -- 5.Function of the MAM -- 5.1.Regulation of lipid metabolisms -- 5.2.Regulation of Ca2+ signaling and bioenergetics -- 5.3.The MAM in mitochondrial trafficking, fusion, and fission -- 5.4.Other potential functions of the MAM -- 6.Significance of the MAM in Cell Physiology and Disease -- 6.1.The MAM in cellular redox and apoptosis -- 6.2.The role of the MAM in the immune response -- 6.3.Implication of the MAM in the pathophysiology of human diseases -- 7.Concluding Remarks -- Acknowledgments -- References -- ch. Three Strategies for Silencing and Escape: The Ancient Struggle Between Transposable Elements and Their Hosts / R. Keith Slotkin -- 1.Introduction -- 2.Basic Description of Types of TEs -- 3.Overview of TE Distributions -- 4.Mechanisms of TE Silencing -- 4.1.Posttranscriptional mechanisms -- 4.2.Transcriptional mechanisms -- 4.3.TE recognition -- 4.4.Maintenance of TE silencing -- 4.5.Zombies in the attic -- 4.6.Spreading the word: TEs and systemic silencing -- 5.Strategies of Evasion -- 5.1.Grab them by the belt -- 5.2.Be a wolf in sheep's clothing -- 5.3.Be a slippery fish -- 5.4.Run away -- 5.5.First do no harm -- 5.6.Earn an honest living -- 5.7.Kick them when they are down -- 5.8.Fight back -- 6.Conclusion: The Semiautonomous Genome -- References -- ch. Four Current Progress and Potential Practical Application for Human Pluripotent Stem Cells / Sergey L. Kiselev -- 1.Introduction -- 2.Biology of Pluripotent Stem Cells -- 2.1.ESCs characteristics -- 2.2.Genetic stability of human ESCs -- 2.3.Molecular mechanisms of pluripotency -- 2.4.Epigenetics of ESCs -- 3.Induced Pluripotent Stem Cells -- 3.1.Genetic reprogramming of somatic cells -- 3.2.Reprogramming with the help of chemical compounds -- 3.3.Genetic stability of iPSCs -- 3.4.Similarity and differences between iPSCs and ESCs -- 3.5.X chromosome inactivation status in human iPSCs -- 4.Biomedical Potential of Human Pluripotent Stem Cells -- 4.1.Differentiation potential of ESCs and iPSCs -- 4.2.Transgene-free iPSCs -- 4.3.Application of iPSCs in model systems -- 5.Concluding Remarks -- References -- ch. Five Protein Quality Control, Retention, and Degradation at the Endoplasmic Reticulum / Gerardo Z. Lederkremer -- 1.Introduction -- 2.ER Retention -- 2.1.Protein translocation into the ER and recognition of misfolded proteins -- 2.2.Mechanisms of retention and retrieval for misfolded proteins -- 2.3.Retention of ER-resident proteins -- 3.Chaperones -- 3.1.ER chaperones -- 3.2.ER-localized Hsp40 chaperones -- 3.3.Oxidoreductases, prolyl isomerases, and disulfide bonds -- 3.4.CNX, CRT, and substrate-specific chaperones -- 4.CNX Cycle -- 4.1.Identification of glycoproteins by CNX and CRT -- 4.2.The opposing roles of GII and GT in the CNX cycle -- 4.3.Release from the CNX cycle -- 5.Mannosidases and Lectins -- 5.1.Mannose trimming -- 5.2.Lectins in ERAD -- 5.3.Mannosidases -- 5.4.Lectins in ER-Golgi transport -- 6.Compartmentalization -- 6.1.MAM, ER stress, and apoptosis -- 6.2.ERES and protein quality control -- 6.3.The ER-derived quality control compartment -- 7.Retrotranslocation -- 7.1.Forward translocation -- 7.2.Current understanding of retrotranslocation -- 7.3.Participating proteins -- 7.4.Pathologies -- 8.ERAD -- 8.1.Ubiquitination -- 8.2.ERAD in yeast and mammalian cells -- 8.3.ERAD of glycoprotein substrates -- 8.4.Degradation of short-lived ERQC components by an autophagic process -- 8.5.Deglycosylation and shuttling to the proteasomes -- 9.ER Stress -- 9.1.The UPR -- 9.2.ER stress-induced apoptosis -- 9.3.The subcellular sites of UPR and ER stress-induced apoptosis -- 10.Concluding Remarks -- Acknowledgment -- References.
Summary:
International Review of Cell and Molecular Biology presents current advances and comprehensive reviews in cell biology--both plant and animal. Articles address structure and control of gene expression, nucleocytoplasmic interactions, control of cell development and differentiation, and cell transformation and growth. Impact factor for 2009: 6.088. * Authored by some of the foremost scientists in the field * Provides up-to-date information and directions for future research * Valuable reference material for advanced undergraduates, graduate students and professional scientists.
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ISBN:
9780123860330 (electronic bk.)
0123860334 (electronic bk.)
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AVAILABLE ONLINE TO AUTHORIZED PSU USERS.
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