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Definition
a cells produce ‘a-factor’, a mating pheromone which signals the presence of an a cell to neighbouring α cells. a cells respond to α-factor, the α cell mating pheromone, by growing a projection (known as a shmoo, due to its distinctive shape) towards the source of α-factor. Similarly, α cells produce α-factor, and respond to a-factor by growing a projection towards the source of the pheromone. The response of haploid cells only to the mating pheromones of the opposite mating type allows mating between a and α cells, but not between cells of the same mating type. |
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Local vs. long-range mediators |
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local mediators are signal molecules that are meant for nearby cells, long range mediators are examples of endocrine signaling. |
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Endocrine, paracrine, juxtacrine signaling |
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Definition
endocrine signaling is the endocrine system (into the blood stream) paracrine is nearby or local signaling juxtacrine requires the cells to be in contact to signal |
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signal triggering molecule that binds to a target site on generally a receptor protein |
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a molecule found on the surface of a cell that accepts signaling molecules for specific functions |
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the process by which an extracellular signaling molecule activates a membrane receptor that in turn alters intracellular molecules creating a response |
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A secondary messenger comes after a primary messenger hahaha, (calcium is a good example of this after the PLC -> IP3 -> ER calcium release |
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Carcinomas, sarcomas, lymphomas, leukemias |
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Definition
Cancers... you should know these if not look em up on wikipedia.. |
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its a tumor, a cancerous mass either benign or malignant |
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hmm think about it, it either stays where it is, or it invades YOUR BODY omg.. |
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Anchorage-independent growth |
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A term used to characterize cells that do not require a solid substratum for growth, i.e., the solid glass or plastic surface of a culture dish or micro-carrier beads. Such cells can be grown in suspension or soft media in which they float freely. |
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Density-dependent inhibition of growth |
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Definition
Cells that run out of nutrition and space and therefore their growth is inhibited think G1 -> S Restriction Point and G2 -> M Checkpoint for growth |
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meta -> next stasis -> placement
displacement, spread of the disease |
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Growth factors typically act as signaling molecules between cells. Examples are cytokines and hormones that bind to specific receptors on the surface of their target cells. They often promote cell differentiation and maturation, which varies between growth factors. For example, bone morphogenic proteins stimulate bone cell differentiation, while fibroblast growth factors and vascular endothelial growth factors stimulate blood vessel differentiation (angiogenesis). |
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Angiogenesis is the physiological process involving the growth of new blood vessels from pre-existing vessels.
Watch the movie, its cool. |
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The nuclear pore complex (NPC), perhaps the largest protein complex in the cell, is responsible for the protected exchange of components between the nucleus and cytoplasm and for preventing the transport of material not destined to cross the nuclear envelope.
http://www.ks.uiuc.edu/Research/npc/ |
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Nuclear localization signal (NLS) |
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Definition
A nuclear localization signal or sequence (NLS) is an amino acid sequence which acts like a 'tag' on the exposed surface of a protein. This sequence is used to target the protein to the cell nucleus through the Nuclear Pore Complex and to direct a newly synthesized protein into the nucleus via its recognition by cytosolic nuclear transport receptors. Typically, this signal consists of one or more short sequences of positively charged lysines or arginines. Different nuclear localized proteins may share the same NLS. An NLS has the opposite function of a nuclear export signal, which targets proteins out of the nucleus. |
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Nuclear export signal (NES) |
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Definition
A nuclear localization signal or sequence (NLS) is an amino acid sequence which acts like a 'tag' on the exposed surface of a protein. This sequence is used to target the protein to the cell nucleus through the Nuclear Pore Complex and to direct a newly synthesized protein into the nucleus via its recognition by cytosolic nuclear transport receptors. Typically, this signal consists of one or more short sequences of positively charged lysines or arginines. Different nuclear localized proteins may share the same NLS. An NLS has the opposite function of a nuclear export signal, which targets proteins out of the nucleus. |
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Nuclear factor of activated T-cells -> binds to calcineurin in high Ca2+ -> activates immune system |
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Ran is a GTP binding protein that is essential for the translocation of RNA and proteins through the nuclear pore complex. The Ran protein is also involved in control of DNA synthesis and cell cycle progression. Nuclear localization of Ran requires the presence of regulator of chromosome condensation 1 (RCC1). Mutations in Ran disrupt DNA synthesis. Because of its many functions, it is likely that Ran interacts with several other proteins.[4] |
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Protein targeting or protein sorting is the mechanism by which a cell transports proteins to the appropriate positions in the cell or outside of it. signal peptide is a short (3-60 amino acids long) peptide chain that directs the transport of a protein. Signal peptides may also be called targeting signals, signal sequences, transit peptides, or localization signals. |
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Signal recognition particle (SRP) |
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Definition
SRP binds to the ER signal sequence and blocks translation then bins to the SRP receptor docking the ribosome on the ER membrane -> GTP binds to SRP and SRP receptor ports is opened -> polypeptide inserted |
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Cotranslational, posttranslational import |
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Definition
The N-terminal signal sequence of the protein is recognized by a signal recognition particle (SRP) while the protein is still being synthesized on the ribosome. The synthesis pauses while the ribosome-protein complex is transferred to a SRP receptor on the endoplasmic reticulum (ER), a membrane-enclosed organelle. There, the nascent protein is inserted into the Sec61 translocation complex (also known as the translocon) that passes through the ER membrane. The signal sequence is immediately cleaved from the polypeptide once it has been translocated into the ER by signal peptidase in secretory proteins.
Even though most proteins are cotranslationally translocated, some are translated in the cytosol and later transported to their destination. This occurs for proteins that go to a mitochondrion, a chloroplast, or a peroxisome (proteins that go to the latter have their signal sequence at the C terminus). Also, proteins targeted for the nucleus are translocated post-translation. They pass through the nuclear envelope via nuclear pores. |
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The translocon (commonly known as a translocator or translocation channel) is the complex of proteins associated with the translocation of nascent polypeptides across membranes. In eukaryotes the polypeptides are transported into the interior (cisternal or luminal) space of the endoplasmic reticulum (ER) from the cytosol. This process requires the protein to cross a hydrophobic lipid bilayer. |
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Protein cleaved after it has been translocated into the ER lumen. |
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Chaperones, BiP, protein disulfide isomerase |
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Internal start transfer sequence |
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GPI (glycophospatidylinositol) anchor |
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Glycosylation is the enzymatic process that attaches glycans to proteins, lipids, or other organic molecules. This enzymatic process produces one of the fundamental biopolymers found in cells (along with DNA, RNA, and proteins). Glycosylation is a form of co-translational and post-translational modification. Glycans serve a variety of structural and functional roles in membrane and secreted proteins.[1] The majority of proteins synthesized in the rough ER undergo glycosylation. It is an enzyme-directed site-specific process, as opposed to the non-enzymatic chemical reaction of glycation. |
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Dolichols play a role the co-translational modification of proteins known as N-glycosylation in the form of dolichol phosphate. Dolichols function as a membrane anchor for the formation of the oligosaccharide Glc3-Man9-GlcNAc2 (where Glc is glucose, Man is mannose, and GlcNAc is N-acetylglucosamine). |
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Golgi apparatus, trans-Golgi network |
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Regulated vs. constitutive secretion |
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Receptor-mediated endocytosis |
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G protein-linked receptor kinase (GRK) |
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regulator of G protein signaling (RGS) |
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pertussis and cholera toxins |
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phosphatidylinostiol-4,5-bisphosphate (PIP2) |
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inositol 1.4.5 trisphosphate (IP3) |
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Calcium waves (intra- and inter-cellular) |
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Calcium-induced calcium release |
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receptor tyrosine kinases (RTKs) |
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epidermal growth factor receptor (EGFR) |
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Ras / MAPK signaling pathway |
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Monomeric G protein (GTPase) |
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GTPase activating protein (GAP) |
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GTPase exchange factor (GEF) |
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fibroblast growth factor receptor (FGFR) |
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constitutively active mutation |
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dominant negative mutation |
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“Plus” and “minus” ends of a microtubule |
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"Barbed" and "pointed" ends of an actin filament |
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Drugs - nocodazole, taxol, cytochalasin, phalloidin |
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Microtubule dynamic instability |
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Gamma tubulin ring complex (γTuRC) |
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Arp2/3-mediated branching |
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Motor Proteins – Kinesin, Dynein, Myosin |
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Sliding Microtubule Model for Cilia |
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Focal contact/focal adhesion |
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Cyclin dependent kinase (Cdk) |
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Retinoblastoma protein (Rb), E2F |
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Anaphase promoting complex (APC), separase, securin, cohesin |
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ATM, Mdm2, p53, p21, Puma |
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Astral and spindle microtubules |
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Trophic (survival) factors |
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Anchorage-dependent growth |
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Anchorage-independent growth |
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Herceptin, tamoxifen, Gleevec, taxol |
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