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140721s2014 caua foab 000 0 eng d |
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|a 9781615045419
|q electronic
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|z 9781615045402
|q paperback
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7 |
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|a 10.4199/C00107ED1V01Y201406BBC007
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| 035 |
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|a (CaBNVSL)cdlls201406bbc007
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|a (OCoLC)884293281
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|a (CaBNVSL)swl00403630
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|a CaBNVSL
|b eng
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|c CaBNVSL
|d CaBNVSL
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4 |
|a QH603.C95
|b M275 2014
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| 100 |
1 |
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|a Marceau, Normand.,
|e author.
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| 245 |
1 |
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|a Intermediate filaments /
|c Normand Marceau, Anne Loranger, and Stéphane Gilbert.
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|a San Rafael, California (1537 Fourth Street, San Rafael, CA 94901 USA) :
|b Morgan & Claypool,
|c 2014.
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| 300 |
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|a 1 PDF (xiii, 112 pages) :
|b illustrations.
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| 336 |
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|a text
|b txt
|2 rdacontent.
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| 337 |
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|a electronic
|2 isbdmedia.
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| 338 |
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|a online resource
|b cr
|2 rdacarrier.
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| 490 |
1 |
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|a Colloquium series on building blocks of the cell,
|x 2328-305X ;
|v # 7.
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| 500 |
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|a Part of: Colloquium digital library of life sciences.
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| 500 |
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|a Series from website.
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|a Includes bibliographical references (pages 75-109)
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|a 1. Introduction --
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|a 2. IFs as a multigene family of filamentous proteins -- 2.1 Evolutionary history -- 2.2 Gene expression and regulation -- 2.2.1 Differential IF gene expression in cells and tissues -- 2.2.2 IF gene regulatory elements -- 2.3 IF protein domains and assembly -- 2.3.1 Common versus diversified domains -- 2.3.2 Subunit assembly and IF dynamics -- 2.4 Post-translational modifications and IF dynamics -- 2.4.1 Phosphorylation -- 2.4.2 Glycosylation -- 2.4.3 Acetylation -- 2.4.4 Sumoylation -- 2.4.5 Transamidation -- 2.4.6 Ubiquitination and degradation -- 2.4.7 Cleavage -- 2.4.8 Other post-translational modifications -- 2.5 IF interactions with cytoskeletal organizers -- 2.5.1 Plectin isoforms as organizers of if architecture -- 2.5.2 APC as IF organizer -- 2.5.3 14-3-3 proteins as IF signaling intermediates -- 2.5.4 Albatross as IF modulator -- 2.6 IF mechanical features and dynamics --
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| 505 |
8 |
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|a 3. Nuclear lamina -- 3.1 Lamin composition -- 3.2 Typical structural features and assembly -- 3.3 Chromatin and nucleo-cytoskeletal interactions --
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| 505 |
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|a 4. IF functional interplay with cell surface domains and organelles -- 4.1 Keratin IFs and desmosomes -- 4.2 Keratin IFs and hemidesmosomes or focal adhesions -- 4.3 Keratin IFs and FAS receptor -- 4.4 Keratin IFs and cell polarity -- 4.5 IF interactions with organelles -- 4.5.1 IFs and mitochondria -- 4.5.2 IFs and GolgI -- 4.5.3 IFs, endosomal-lysosomal sorting machinery, and autophagosomes --
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|a 5. IFs and cell specialization -- 5.1 Differentiation -- 5.1.1 IF sequential expression from embryonic to mature tissue -- 5.1.2 IFs and cell differentiation -- 5.2 Proliferation, cell size, and protein synthesis -- 5.3 Migration and cell stiffness -- 5.4 IFs and cellular stress responses -- 5.4.1 Mechanical stress -- 5.4.2 Apoptosis -- 5.4.3 Chemical and oxidative stress -- 5.4.4 Other stresses -- 5.5 IFs and signal transduction -- 5.5.1 MAPK/ERK pathway -- 5.5.2 SAPK/JNK pathway -- 5.5.3 PI3K/Akt pathway -- 5.5.4 PKCs and p38 MAPK pathway -- 5.5.5 Other signaling pathways -- 5.6 IFs in metabolism --
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|a 6. IF relevance to human diseases -- 6.1 Keratin IF-pathies -- 6.2 Neuro IF-pathies -- 6.3 Desminopathy -- 6.4 Laminopathies --
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8 |
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|a 7. Conclusion -- References-- Author biographies.
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3 |
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|a Intermediate filaments (IFs), in concert with microfilaments (MFs) and microtubules (MTs), form the cytoskeleton, and each of these fibrillar networks exhibits rather unique structural and functional characteristics. Intermediate filaments were discovered in eukaryotic cells in the late 1960s, and their name comes from the fact that their diameter is intermediate between MFs and MTs. In contrast to the latter, IFs constitute a network that extends from the nuclear envelope throughout the cytoplasm, and in many cases, interact with cell surface domains involved in cell-cell and cell- matrix interactions. Several key features of their expression, assembly, structure and dynamics are highlighted in this eBook. For instance, IF proteins are encoded by several genes, which are classified into six types reflecting the tissues (cells) of origin. Moreover, IF proteins contain a conserved central a-helical (rod) domain flanked by N-terminal (head) and C-terminal (tail) globular domains that enables assembly of fibrous IFs exhibiting a tripartite structure. Although the rod domain is responsible for the formation of the coiled-coil framework and yields the main driving force during the IF protein assembly, the head and tail domains contribute to most of the structural heterogeneity of IF organization and undergo several types of post-translational modifications. Furthermore, the development of gene targeting methods to genetically knockout the expression of the IF genes in mice has uncovered the mechanical versus non-mechanical features of the IF networks, namely, their involvement in cell response to diverse forms of stress, growth stimulation, migration, or death insults. Finally, there is accumulating evidence revealing that the tissue and cell-type expression of IF genes reflects itself in the presence of causal or predisposition mutations responsible for numerous human tissue-specific diseases, known as IF-pathies.
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| 538 |
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|a Mode of access: World Wide Web.
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| 538 |
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|a System requirements: Adobe Acrobat reader.
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| 588 |
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|a Title from PDF title page (viewed on July 21, 2014)
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| 650 |
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|a Cytoplasmic filaments.
|0 http://id.loc.gov/authorities/subjects/sh85035252.
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| 700 |
1 |
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|a Loranger, Anne.,
|e author.
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| 700 |
1 |
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|a Gilbert, Stéphane.,
|e author.
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| 776 |
0 |
8 |
|i Print version:
|z 9781615045402.
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| 830 |
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|a Colloquium series on building blocks of the cell ;
|v # 7.
|0 http://id.loc.gov/authorities/names/no2013125588.
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| 856 |
4 |
8 |
|3 Abstract with links to full text
|u https://colorado.idm.oclc.org/login?url=http://dx.doi.org/10.4199/C00107ED1V01Y201406BBC007
|z Full Text (via Colloquium Digital Library)
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