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Formin
Formins (formin homology proteins) are a group of proteins that are involved in the polymerization of actin and associate with the fast-growing end (barbed end) of actin filaments. Most formins are Rho-GTPase effector proteins. Formins regulate the actin and microtubule cytoskeleton and are involved in various cellular functions such as cell polarity, cytokinesis, cell migration and SRF transcriptional activity. Formins are multidomain proteins that interact with diverse signalling molecules and cytoskeletal proteins, although some formins have been assigned functions within the nucleus. Diversity Formins have been found in all eukaryotes studied. In humans, 15 different formin proteins are present that have been classified in 7 subgroups. By contrast, yeasts contain only 2-3 formins. Structure and interactions Formins are characterized by the presence of three formin homology (FH) domains (FH1, FH2 and FH3), although members of the formin family do not neces ...
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Actin
Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42  kDa, with a diameter of 4 to 7 nm. An actin protein is the monomeric subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the contractile apparatus in muscle cells. It can be present as either a free monomer called G-actin (globular) or as part of a linear polymer microfilament called F-actin (filamentous), both of which are essential for such important cellular functions as the mobility and contraction of cells during cell division. Actin participates in many important cellular processes, including muscle contraction, cell motility, cell division and cytokinesis, vesicle and organelle mov ...
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Cell Polarity
Cell polarity refers to spatial differences in shape, structure, and function within a cell. Almost all cell types exhibit some form of polarity, which enables them to carry out specialized functions. Classical examples of polarized cells are described below, including epithelial cells with apical-basal polarity, neurons in which signals propagate in one direction from dendrites to axons, and migrating cells. Furthermore, cell polarity is important during many types of asymmetric cell division to set up functional asymmetries between daughter cells. Many of the key molecular players implicated in cell polarity are well conserved. For example, in metazoan cells, the complex plays a fundamental role in cell polarity. While the biochemical details may vary, some of the core principles such as negative and/or positive feedback between different molecules are common and essential to many known polarity systems. Examples of polarized cells Epithelial cells Epithelial cells adhe ...
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Actin-binding Protein
Actin-binding proteins (also known as ABPs) are proteins that bind to actin. This may mean ability to bind actin monomers, or polymers, or both. Many actin-binding proteins, including α-actinin, β-spectrin, dystrophin, utrophin and fimbrin, do this through the actin-binding calponin homology domain. This is a list of actin-binding proteins in alphabetical order. 0–9 * 25kDa * 25kDa ABP from aorta * 30akDA * 30bkDa * 34kDA * 45kDa * 110 kD dimer ABP * 110 kD ( Drebrin) * p53 * p58gag * p185neu * p116rip A * a-actinin * Abl * ABLIM *Actin-Interacting MAPKKK Ssk2p * ABP120 * ABP140 * Abp1p * ABP280 ( Filamin) * ABP50 (EF-1a) * Acan 125 (Carmil) * ActA * Actibind *Actin * Actinfilin * Actinogelin * Actin-regulating kinases * Actin-Related Proteins * Actobindin * Actolinkin * Actopaxin * Actophorin * Acumentin (= L- plastin) * Adducin * ADF/Cofilin * Adseverin (scinderin) * Afadin * AFAP-110 * Affixin * Aginactin * AIP1 * Aldolase * Angiogenin * Anillin * Annexins * Ap ...
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Yeast
Yeasts are eukaryotic, single-celled microorganisms classified as members of the fungus kingdom (biology), kingdom. The first yeast originated hundreds of millions of years ago, and at least 1,500 species are currently recognized. They are estimated to constitute 1% of all described fungal species. Some yeast species have the ability to develop multicellular characteristics by forming strings of connected budding cells known as pseudohyphae or false hyphae, or quickly evolve into a Multicellular organism, multicellular cluster with specialised Organelle, cell organelles function. Yeast sizes vary greatly, depending on species and environment, typically measuring 3–4 micrometre, μm in diameter, although some yeasts can grow to 40 μm in size. Most yeasts reproduce asexual reproduction, asexually by mitosis, and many do so by the asymmetric division process known as budding. With their single-celled growth habit, yeasts can be contrasted with Mold (fungus), molds, wh ...
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Intracellular
This glossary of biology terms is a list of definitions of fundamental terms and concepts used in biology, the study of life and of living organisms. It is intended as introductory material for novices; for more specific and technical definitions from sub-disciplines and related fields, see Glossary of cell biology, Glossary of genetics, Glossary of evolutionary biology, Glossary of ecology, Glossary of environmental science and Glossary of scientific naming, or any of the organism-specific glossaries in :Glossaries of biology. A B C D E ...
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Conserved Sequence
In evolutionary biology, conserved sequences are identical or similar sequences in nucleic acids ( DNA and RNA) or proteins across species ( orthologous sequences), or within a genome ( paralogous sequences), or between donor and receptor taxa ( xenologous sequences). Conservation indicates that a sequence has been maintained by natural selection. A highly conserved sequence is one that has remained relatively unchanged far back up the phylogenetic tree, and hence far back in geological time. Examples of highly conserved sequences include the RNA components of ribosomes present in all domains of life, the homeobox sequences widespread amongst eukaryotes, and the tmRNA in bacteria. The study of sequence conservation overlaps with the fields of genomics, proteomics, evolutionary biology, phylogenetics, bioinformatics and mathematics. History The discovery of the role of DNA in heredity, and observations by Frederick Sanger of variation between animal insulins in 194 ...
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Enzyme Inhibitor
An enzyme inhibitor is a molecule that binds to an enzyme and blocks its Enzyme activity, activity. Enzymes are proteins that speed up chemical reactions necessary for life, in which Substrate (biochemistry), substrate molecules are converted into Product (chemistry), products. An enzyme Enzyme catalysis, facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the enzyme that accelerates the Rate-determining step, most difficult step of the reaction. An enzyme inhibitor stops ("inhibits") this process, either by binding to the enzyme's active site (thus preventing the substrate itself from binding) or by binding to another site on the enzyme such that the enzyme's catalysis of the reaction is blocked. Enzyme inhibitors may bind Reversible reaction, reversibly or irreversibly. Irreversible inhibitors form a Covalent bond, chemical bond with the enzyme such that the enzyme is inhibited until the chemical bond is broken. By cont ...
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Saccharomyces Cerevisiae
''Saccharomyces cerevisiae'' () (brewer's yeast or baker's yeast) is a species of yeast (single-celled fungal microorganisms). The species has been instrumental in winemaking, baking, and brewing since ancient times. It is believed to have been originally isolated from the skin of grapes. It is one of the most intensively studied eukaryotic model organisms in molecular and cell biology, much like '' Escherichia coli'' as the model bacterium. It is the microorganism which causes many common types of fermentation. ''S. cerevisiae'' cells are round to ovoid, 5–10  μm in diameter. It reproduces by budding. Many proteins important in human biology were first discovered by studying their homologs in yeast; these proteins include cell cycle proteins, signaling proteins, and protein-processing enzymes. ''S. cerevisiae'' is currently the only yeast cell known to have Berkeley bodies present, which are involved in particular secretory pathways. Antibodies again ...
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WW Domain
The WW domain (also known as the rsp5-domain or WWP repeating structural motif, motif) is a modular protein domain that mediates specific interactions with protein ligands. This domain is found in a number of unrelated signaling and structural proteins and may be repeated up to four times in some proteins. Apart from binding preferentially to proteins that are proline-rich, with particular proline-motifs, [AP]-P-P-[AP]-Y, some WW domains bind to phosphoserine- and phosphothreonine-containing motifs. Structure and ligands The WW domain is one of the smallest protein modules, composed of only 40 amino acids, which mediates specific protein-protein interactions with short proline-rich or proline-containing motifs. Named after the presence of two conserved tryptophans (W), which are spaced 20-22 amino acids apart within the sequence, the WW domain folds into a meandering triple-stranded beta sheet. The identification of the WW domain was facilitated by the analysis of two splice ...
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SH3 Domain
The SRC Homology 3 Domain (or SH3 domain) is a small protein domain of about 60 amino acid residues. Initially, SH3 was described as a conserved sequence in the viral adaptor protein v-Crk. This domain is also present in the molecules of phospholipase and several cytoplasmic tyrosine kinases such as Abl and Src. It has also been identified in several other protein families such as: PI3 Kinase, Ras GTPase-activating protein, CDC24 and cdc25. SH3 domains are found in proteins of signaling pathways regulating the cytoskeleton, the Ras protein, and the Src kinase and many others. The SH3 proteins interact with adaptor proteins and tyrosine kinases. Interacting with tyrosine kinases, SH3 proteins usually bind far away from the active site. Approximately 300 SH3 domains are found in proteins encoded in the human genome. In addition to that, the SH3 domain was responsible for controlling protein-protein interactions in the signal transduction pathways and regulating the ...
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Profilin
Profilin is an actin-binding protein involved in the dynamic turnover and reconstruction of the actin cytoskeleton. It is found in most eukaryotic organisms. Profilin is important for spatially and temporally controlled growth of actin microfilaments, which is an essential process in cellular locomotion and cell shape changes. This restructuring of the actin cytoskeleton is essential for processes such as organ development, wound healing, and the hunting down of infectious intruders by cells of the immune system. Profilin also binds sequences rich in the amino acid proline in diverse proteins. While most profilin in the cell is bound to actin, profilins have over 50 different binding partners. Many of those are related to actin regulation, but profilin also seems to be involved in activities in the nucleus such as mRNA splicing. Profilin is the major allergen (via IgE) present in birch, grass, and other pollen. Sources and distribution Profilins are proteins of molecular weig ...
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