Securin Phosphorylation Sites2
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Securin Phosphorylation Sites2
Securin is a protein involved in control of the metaphase-anaphase transition and anaphase onset. Following bi-orientation of chromosome pairs and inactivation of the spindle checkpoint system, the underlying regulatory system, which includes securin, produces an abrupt stimulus that induces highly synchronous chromosome separation in anaphase. Securin and Separase Securin is initially present in the cytoplasm and binds to separase, a protease that degrades the cohesin rings that link the two sister chromatids. Separase is vital for onset of anaphase. This securin-separase complex is maintained when securin is phosphorylated by Cdk1, inhibiting ubiquitination. When bound to securin, separase is not functional. In addition, both securin and separase are well-conserved proteins (Figure 1). Note that separase cannot function without initially forming the securin-separase complex. This is because securin helps properly fold separase into the functional conformation. However, yeast ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ...
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Chromosome
A chromosome is a long DNA molecule with part or all of the genetic material of an organism. In most chromosomes the very long thin DNA fibers are coated with packaging proteins; in eukaryotic cells the most important of these proteins are the histones. These proteins, aided by chaperone proteins, bind to and condense the DNA molecule to maintain its integrity. These chromosomes display a complex three-dimensional structure, which plays a significant role in transcriptional regulation. Chromosomes are normally visible under a light microscope only during the metaphase of cell division (where all chromosomes are aligned in the center of the cell in their condensed form). Before this happens, each chromosome is duplicated ( S phase), and both copies are joined by a centromere, resulting either in an X-shaped structure (pictured above), if the centromere is located equatorially, or a two-arm structure, if the centromere is located distally. The joined copies are now called si ...
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Anaphase
Anaphase () is the stage of mitosis after the process of metaphase, when replicated chromosomes are split and the newly-copied chromosomes (daughter chromatids) are moved to opposite poles of the cell. Chromosomes also reach their overall maximum condensation in late anaphase, to help chromosome segregation and the re-formation of the nucleus. Anaphase starts when the anaphase promoting complex marks an inhibitory chaperone called securin for destruction by ubiquinylating it. Securin is a protein which inhibits a protease known as separase. The destruction of securin unleashes separase which then breaks down cohesin, a protein responsible for holding sister chromatids together. At this point, three subclasses of microtubule unique to mitosis are involved in creating the forces necessary to separate the chromatids: kinetochore microtubules, interpolar microtubules, and astral microtubules. The centromeres are split, and the sister chromatids are pulled toward the poles by ki ...
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Separase
Separase, also known as separin, is a cysteine protease responsible for triggering anaphase by hydrolysing cohesin, which is the protein responsible for binding sister chromatids during the early stage of anaphase. In humans, separin is encoded by the ''ESPL1'' gene. History In ''S. cerevisiae'', separase is encoded by the ''esp1'' gene. Esp1 was discovered by Kim Nasmyth and coworkers in 1998. In 2021, structures of human separase were determined in complex with either securin or CDK1-cyclin B1-CKS1 using cryo-EM by scientists of the University of Geneva. Function Stable cohesion between sister chromatids before anaphase and their timely separation during anaphase are critical for cell division and chromosome inheritance. In vertebrates, sister chromatid cohesion is released in 2 steps via distinct mechanisms. The first step involves phosphorylation of STAG1 or STAG2 in the cohesin complex. The second step involves cleavage of the cohesin subunit SCC1 ( RAD21) by separase, ...
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Protease
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes (increases reaction rate or "speeds up") proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in many biological functions, including digestion of ingested proteins, protein catabolism (breakdown of old proteins), and cell signaling. In the absence of functional accelerants, proteolysis would be very slow, taking hundreds of years. Proteases can be found in all forms of life and viruses. They have independently evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Hierarchy of proteases Based on catalytic residue Proteases can be classified into seven broad groups: * Serine protease ...
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Cdk1
Cyclin-dependent kinase 1 also known as CDK1 or cell division cycle protein 2 homolog is a highly conserved protein that functions as a serine/threonine protein kinase, and is a key player in cell cycle regulation. It has been highly studied in the budding yeast ''S. cerevisiae'', and the fission yeast ''S. pombe'', where it is encoded by genes ''cdc28'' an''cdc2'' respectively. With its cyclin partners, Cdk1 forms complexes that phosphorylate a variety of target substrates (over 75 have been identified in budding yeast); phosphorylation of these proteins leads to cell cycle progression. Structure Cdk1 is a small protein (approximately 34 kilodaltons), and is highly conserved. The human homolog of Cdk1, ''CDK1'', shares approximately 63% amino-acid identity with its yeast homolog. Furthermore, human ''CDK1'' is capable of rescuing fission yeast carrying a ''cdc2'' mutation. Cdk1 is comprised mostly by the bare protein kinase motif, which other protein kinases share. Cdk1, li ...
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Securin Phosphorylation Sites2
Securin is a protein involved in control of the metaphase-anaphase transition and anaphase onset. Following bi-orientation of chromosome pairs and inactivation of the spindle checkpoint system, the underlying regulatory system, which includes securin, produces an abrupt stimulus that induces highly synchronous chromosome separation in anaphase. Securin and Separase Securin is initially present in the cytoplasm and binds to separase, a protease that degrades the cohesin rings that link the two sister chromatids. Separase is vital for onset of anaphase. This securin-separase complex is maintained when securin is phosphorylated by Cdk1, inhibiting ubiquitination. When bound to securin, separase is not functional. In addition, both securin and separase are well-conserved proteins (Figure 1). Note that separase cannot function without initially forming the securin-separase complex. This is because securin helps properly fold separase into the functional conformation. However, yeast ...
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Cdc14
''Cdc14'' and Cdc14 are a gene and its protein product respectively. Cdc14 is found in most of the eukaryotes. Cdc14 was defined by Hartwell in his famous screen for loci that control the cell cycle of Saccharomyces cerevisiae. Cdc14 was later shown to encode a protein phosphatase. Cdc14 is dual-specificity, which means it has serine/threonine and tyrosine-directed activity. A preference for serines next to proline is reported. Many early studies, especially in the budding yeast Saccharomyces cerevisiae, demonstrated that the protein plays a key role in regulating late mitotic processes. However, more recent work in a range of systems suggests that its cellular function is more complex. Cellular function In Saccharomyces cerevisiae, the species in which Cdc14 activity is best understood and most-studied, the activity of Cdc14 (ScCdc14) leads to mitotic exit by dephosphorylating targets of Cdk1, a well-studied cyclin-dependent protein kinase. Cdc14 antagonizes Cdk1 by stimula ...
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Cdc20
The cell division cycle protein 20 homolog is an essential regulator of cell division that is encoded by the ''CDC20'' gene in humans. To the best of current knowledge its most important function is to activate the anaphase promoting complex (APC/C), a large 11-13 subunit complex that initiates chromatid separation and entrance into anaphase. The APC/CCdc20 protein complex has two main downstream targets. Firstly, it targets securin for destruction, enabling the eventual destruction of cohesin and thus sister chromatid separation. It also targets S and M-phase (S/M) cyclins for destruction, which inactivates S/M cyclin-dependent kinases (Cdks) and allows the cell to exit from mitosis. A closely related protein, Cdc20homologue-1 (Cdh1) plays a complementary role in the cell cycle. CDC20 appears to act as a regulatory protein interacting with many other proteins at multiple points in the cell cycle. It is required for two microtubule-dependent processes: nuclear movement prior to an ...
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Network Picture
Network, networking and networked may refer to: Science and technology * Network theory, the study of graphs as a representation of relations between discrete objects * Network science, an academic field that studies complex networks Mathematics * Networks, a graph with attributes studied in network theory ** Scale-free network, a network whose degree distribution follows a power law ** Small-world network, a mathematical graph in which most nodes are not neighbors, but have neighbors in common * Flow network, a directed graph where each edge has a capacity and each edge receives a flow Biology * Biological network, any network that applies to biological systems * Ecological network, a representation of interacting species in an ecosystem * Neural network, a network or circuit of neurons Technology and communication * Artificial neural network, a computing system inspired by animal brains * Broadcast network, radio stations, television stations, or other electronic media outlets ...
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Positive Feedback
Positive feedback (exacerbating feedback, self-reinforcing feedback) is a process that occurs in a feedback loop which exacerbates the effects of a small disturbance. That is, the effects of a perturbation on a system include an increase in the magnitude of the perturbation. That is, ''A produces more of B which in turn produces more of A''.Keesing, R.M. (1981). Cultural anthropology: A contemporary perspective (2nd ed.) p.149. Sydney: Holt, Rinehard & Winston, Inc. In contrast, a system in which the results of a change act to reduce or counteract it has negative feedback. Both concepts play an important role in science and engineering, including biology, chemistry, and cybernetics. Mathematically, positive feedback is defined as a positive loop gain around a closed loop of cause and effect. That is, positive feedback is Phase (waves), in phase with the input, in the sense that it adds to make the input larger. Positive feedback tends to cause Control theory#Stability, system i ...
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