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RALB
Ras-related protein Ral-B (RalB) is a protein that in humans is encoded by the ''RALB'' gene on chromosome 2. This protein is one of two paralogs of the Ral protein, the other being RalA, and part of the Ras GTPase family. RalA functions as a molecular switch to activate a number of biological processes, majorly cell division and transport, via signaling pathways. Its biological role thus implicates it in many cancers. Structure The Ral isoforms share an 80% overall match in amino acid sequence and 100% match in their effector-binding region. The two isoforms mainly differ in the C-terminal hypervariable region, which contains multiple sites for post-translational modification, leading to diverging subcellular localization and biological function. For example, phosphorylation of Serine 194 on RalA by the kinase Aurora A results in the relocation of RalA to the inner mitochondrial membrane, where RalA helps carry out mitochondrial fission; whereas phosphorylation of Serine 198 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RALBP1
RalA-binding protein 1 is a protein that in humans is encoded by the ''RALBP1'' gene. Interactions RALBP1 has been shown to interact with: * Cyclin B1, * HSF1, * RALA, * RALB, and * REPS2 RalBP1-associated Eps domain-containing protein 2 is a protein that in humans is encoded by the ''REPS2'' gene. Function The product of this gene is part of a protein complex that regulates the endocytosis of growth factor receptors. The .... References Further reading * * * * * * * * * * * * * * * * * {{gene-18-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RALA
Ras-related protein Ral-A (RalA) is a protein that in humans is encoded by the ''RALA'' gene on chromosome 7. This protein is one of two paralogs of the Ral protein, the other being RalB, and part of the Ras GTPase family. RalA functions as a molecular switch to activate a number of biological processes, majorly cell division and transport, via signaling pathways. Its biological role thus implicates it in many cancers. Structure The Ral isoforms share an 80% overall match in amino acid sequence and 100% match in their effector-binding region. The two isoforms mainly differ in the C-terminal hypervariable region, which contains multiple sites for post-translational modification, leading to diverging subcellular localization and biological function. For example, phosphorylation of Serine 194 on RalA by the kinase Aurora A results in the relocation of RalA to the inner mitochondrial membrane, where RalA helps carry out mitochondrial fission; whereas phosphorylation of Serine 198 on ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EXOC8
Exocyst complex component 8 is a protein that in humans is encoded by the ''EXOC8'' gene. Interactions EXOC8 has been shown to interact with RALB Ras-related protein Ral-B (RalB) is a protein that in humans is encoded by the ''RALB'' gene on chromosome 2. This protein is one of two paralogs of the Ral protein, the other being RalA, and part of the Ras GTPase family. RalA functions as a m .... References Further reading * * * * * * * {{gene-1-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TANK-binding Kinase 1
TBK1 (TANK-binding kinase 1) is an enzyme with kinase activity. Specifically, it is a serine / threonine protein kinase. It is encoded by the TBK1 gene in humans. This kinase is mainly known for its role in innate immunity antiviral response. However, TBK1 also regulates cell proliferation, apoptosis, autophagy, and anti-tumor immunity. Insufficient regulation of TBK1 activity leads to autoimmune, neurodegenerative diseases or tumorigenesis. Structure and regulation of activity TBK1 is a non-canonical IKK kinase that phosphorylates the nuclear factor kB (NFkB). It shares sequence homology with canonical IKK. The N-terminus of the protein contains the kinase domain (region 9-309) and the ubiquitin-like domain (region 310-385). The C-terminus is formed by two coiled-coil structures (region 407-713) that provide a surface for homodimerization. The autophosphorylation of serine 172, which requires homodimerization and ubiquitinylation of lysines 30 and 401, is necessary for kinase ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytokinesis
Cytokinesis () is the part of the cell division process during which the cytoplasm of a single eukaryotic cell divides into two daughter cells. Cytoplasmic division begins during or after the late stages of nuclear division in mitosis and meiosis. During cytokinesis the spindle apparatus partitions and transports duplicated chromatids into the cytoplasm of the separating daughter cells. It thereby ensures that chromosome number and complement are maintained from one generation to the next and that, except in special cases, the daughter cells will be functional copies of the parent cell. After the completion of the telophase and cytokinesis, each daughter cell enters the interphase of the cell cycle. Particular functions demand various deviations from the process of symmetrical cytokinesis; for example in oogenesis in animals the ovum takes almost all the cytoplasm and organelles. This leaves very little for the resulting polar bodies, which in most species die without fu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Filopodia
Filopodia (singular filopodium) are slender cytoplasmic projections that extend beyond the leading edge of lamellipodia in migrating cells. Within the lamellipodium, actin ribs are known as ''microspikes'', and when they extend beyond the lamellipodia, they're known as filopodia. They contain microfilaments (also called actin filaments) cross-linked into bundles by actin-bundling proteins, such as fascin and fimbrin. Filopodia form focal adhesions with the substratum, linking them to the cell surface. Many types of migrating cells display filopodia, which are thought to be involved in both sensation of chemotropic cues, and resulting changes in directed locomotion. Activation of the Rho family of GTPases, particularly cdc42 and their downstream intermediates, results in the polymerization of actin fibers by Ena/Vasp homology proteins. Growth factors bind to receptor tyrosine kinases resulting in the polymerization of actin filaments, which, when cross-linked, make up the s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tight Junction
Tight junctions, also known as occluding junctions or ''zonulae occludentes'' (singular, ''zonula occludens''), are multiprotein junctional complexes whose canonical function is to prevent leakage of solutes and water and seals between the epithelial cells. They also play a critical role maintaining the structure and permeability of endothelial cells. Tight junctions may also serve as leaky pathways by forming selective channels for small cations, anions, or water. The corresponding junctions that occur in invertebrates are septate junctions. Structure Tight junctions are composed of a branching network of sealing strands, each strand acting independently from the others. Therefore, the efficiency of the junction in preventing ion passage increases exponentially with the number of strands. Each strand is formed from a row of transmembrane proteins embedded in both plasma membranes, with extracellular domains joining one another directly. There are at least 40 different protei ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Receptor-mediated Endocytosis
Receptor-mediated endocytosis (RME), also called clathrin-mediated endocytosis, is a process by which cells absorb metabolites, hormones, proteins – and in some cases viruses – by the inward budding of the plasma membrane ( invagination). This process forms vesicles containing the absorbed substances and is strictly mediated by receptors on the surface of the cell. Only the receptor-specific substances can enter the cell through this process. Process Although receptors and their ligands can be brought into the cell through a few mechanisms (e.g. caveolin and lipid raft), clathrin-mediated endocytosis remains the best studied. Clathrin-mediated endocytosis of many receptor types begins with the ligands binding to receptors on the cell plasma membrane. The ligand and receptor will then recruit adaptor proteins and clathrin triskelions to the plasma membrane around where invagination will take place. Invagination of the plasma membrane then occurs, forming a clathrin-coated p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Exocytosis
Exocytosis () is a form of active transport and bulk transport in which a cell transports molecules (e.g., neurotransmitters and proteins) out of the cell ('' exo-'' + ''cytosis''). As an active transport mechanism, exocytosis requires the use of energy to transport material. Exocytosis and its counterpart, endocytosis, are used by all cells because most chemical substances important to them are large polar molecules that cannot pass through the hydrophobic portion of the cell membrane by passive means. Exocytosis is the process by which a large amount of molecules are released; thus it is a form of bulk transport. Exocytosis occurs via secretory portals at the cell plasma membrane called porosomes. Porosomes are permanent cup-shaped lipoprotein structure at the cell plasma membrane, where secretory vesicles transiently dock and fuse to release intra-vesicular contents from the cell. In exocytosis, membrane-bound secretory vesicles are carried to the cell membrane, where ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Autophagosome
An autophagosome is a spherical structure with double layer membranes. It is the key structure in macroautophagy, the intracellular degradation system for cytoplasmic contents (e.g., abnormal intracellular proteins, excess or damaged organelles, invading microorganisms). After formation, autophagosomes deliver cytoplasmic components to the lysosomes. The outer membrane of an autophagosome fuses with a lysosome to form an autolysosome. The lysosome's hydrolases degrade the autophagosome-delivered contents and its inner membrane. The formation of autophagosomes is regulated by genes that are well-conserved from yeast to higher eukaryotes. The nomenclature of these genes has differed from paper to paper, but it has been simplified in recent years. The gene families formerly known as APG, AUT, CVT, GSA, PAZ, and PDD are now unified as the ATG (AuTophaGy related) family. The size of autophagosomes vary between mammals and yeast. Yeast autophagosomes are about 500-900 nm, while m ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
