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ILK
Integrin-linked kinase is an enzyme that in humans is encoded by the ILK gene involved with integrin-mediated signal transduction. Mutations in ''ILK'' are associated with cardiomyopathies. It is a 59kDa protein originally identified in a yeast-two hybrid screen with integrin β1 as the bait protein. Since its discovery, ILK has been associated with multiple cellular functions including cell migration, proliferation, and adhesion. Integrin-linked kinases (ILKs) are a subfamily of Raf-like kinases (RAF). The structure of ILK consists of three features: 5 ankyrin repeats in the N-terminus, Phosphoinositide binding motif and extreme N-terminus of kinase catalytic domain. Integrins lack enzymatic activity and depend on adapters to signal proteins. ILK is linked to beta-1 and beta-3 integrin cytoplasmic domains and is one of the best described integrins. Although first described as a serine/threonine kinase by Hannigan, important motifs of ILK kinases are still uncharacterized. ILK is ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ILKAP
Integrin-linked kinase-associated serine/threonine phosphatase 2C is an enzyme that in humans is encoded by the ''ILKAP'' gene. The protein encoded by this gene is a protein serine/threonine phosphatase of the PP2C family. This protein can interact with integrin-linked kinase (ILK/ILK1), a regulator of integrin mediated signaling, and regulate the kinase activity of ILK. Through the interaction with ILK, this protein may selectively affect the signaling process of ILK-mediated glycogen synthase kinase 3 beta (GSK3beta), and thus participate in Wnt signaling pathway. Interactions ILKAP has been shown to interact with Integrin-linked kinase Integrin-linked kinase is an enzyme that in humans is encoded by the ILK gene involved with integrin-mediated signal transduction. Mutations in ''ILK'' are associated with cardiomyopathies. It is a 59kDa protein originally identified in a yeast-two .... References Further reading * * * * * {{gene-2-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HAK5
High Affinity K+ transporter HAK5 is a transport protein found on the cell surface membrane of plants under conditions of potassium deprivation. It is believed to act as a symporter for protons and the potassium ion, K+. Firstly discovered in barley, receiving the name of HvHAK1, it was soon after identified in the model plant Arabidopsis thaliana and named HAK5. These transporters belongs to the subgroup I of the KT-HAK-KUP family of plant proteins with obvious homology with both bacterial and fungal transport systems, which experienced a major diversification following land conquest. KT-HAK-KUP transporters are one of four different types of K+ transporter within the cell, but are unique as they do not have a putative pore forming domain like the other three; Shaker channels, KCO channels, HKT transporters. It is activated when the plant is situated in low soil with low potassium concentration, and has been shown to be located in higher concentration in the epidermis and vasculat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Signal Transduction
Signal transduction is the process by which a chemical or physical signal is transmitted through a cell as a series of molecular events, most commonly protein phosphorylation catalyzed by protein kinases, which ultimately results in a cellular response. Proteins responsible for detecting stimuli are generally termed receptors, although in some cases the term sensor is used. The changes elicited by ligand binding (or signal sensing) in a receptor give rise to a biochemical cascade, which is a chain of biochemical events known as a signaling pathway. When signaling pathways interact with one another they form networks, which allow cellular responses to be coordinated, often by combinatorial signaling events. At the molecular level, such responses include changes in the transcription or translation of genes, and post-translational and conformational changes in proteins, as well as changes in their location. These molecular events are the basic mechanisms controlling cell growth, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
LIMS1
LIM and senescent cell antigen-like-containing domain protein 1 is a protein that in humans is encoded by the ''LIMS1'' gene. Function The protein encoded by this gene is an adaptor protein which contains five LIM domains, or double zinc fingers. The protein is likely involved in integrin signaling through its LIM domain-mediated interaction with integrin-linked kinase, found in focal adhesion plaques. It is also thought to act as a bridge linking integrin-linked kinase to NCK adaptor protein 2, which is involved in growth factor receptor kinase signaling pathways. Its localization to the periphery of spreading cells also suggests that this protein may play a role in integrin-mediated cell adhesion or spreading. Interactions LIMS1 has been shown to interact with Integrin-linked kinase and NCK2 Cytoplasmic protein NCK2 (also known as NCK-beta and Grb4) is a protein that in humans is encoded by the ''NCK2'' gene. Function NCK belongs to family of adaptor proteins. There a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AKT1
RAC(Rho family)-alpha serine/threonine-protein kinase is an enzyme that in humans is encoded by the ''AKT1'' gene. This enzyme belongs to the AKT subfamily of serine/threonine kinases that contain SH2 (Src homology 2-like) protein domains. It is commonly referred to as PKB, or by both names as "Akt/PKB". Function The serine-threonine protein kinase AKT1 is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase. In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Centrosome
In cell biology, the centrosome (Latin centrum 'center' + Greek sōma 'body') (archaically cytocentre) is an organelle that serves as the main microtubule organizing center (MTOC) of the animal cell, as well as a regulator of cell-cycle progression. The centrosome provides structure for the cell. The centrosome is thought to have evolved only in the metazoan lineage of eukaryotic cells. Fungi and plants lack centrosomes and therefore use other structures to organize their microtubules. Although the centrosome has a key role in efficient mitosis in animal cells, it is not essential in certain fly and flatworm species. Centrosomes are composed of two centrioles arranged at right angles to each other, and surrounded by a dense, highly structured mass of protein termed the pericentriolar material (PCM). The PCM contains proteins responsible for microtubule nucleation and anchoring — including γ-tubulin, pericentrin and ninein. In general, each centriole of the centrosome is based ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Reactive Oxygen Species
In chemistry, reactive oxygen species (ROS) are highly reactive chemicals formed from diatomic oxygen (). Examples of ROS include peroxides, superoxide, hydroxyl radical, singlet oxygen, and alpha-oxygen. The reduction of molecular oxygen () produces superoxide (), which is the precursor to most other reactive oxygen species: :O2 + e^- -> \ ^\bullet O2- Dismutation of superoxide produces hydrogen peroxide (): :2 H+ + \ ^\bullet O2^- + \ ^\bullet O2^- -> H2O2 + O2 Hydrogen peroxide in turn may be partially reduced, thus forming hydroxide ions and hydroxyl radicals (), or fully reduced to water: :H2O2 + e^- -> HO^- + \ ^\bullet OH :2 H+ + 2 e- + H2O2 -> 2 H2O In a biological context, ROS are byproducts of the normal metabolism of oxygen. ROS have roles in cell signaling and homeostasis. ROS are intrinsic to cellular functioning, and are present at low and stationary levels in normal cells. In plants, ROS are involved in metabolic processes related to photoprotection and toleran ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Plant ILK Structural Features
Plants are predominantly photosynthetic eukaryotes of the kingdom Plantae. Historically, the plant kingdom encompassed all living things that were not animals, and included algae and fungi; however, all current definitions of Plantae exclude the fungi and some algae, as well as the prokaryotes (the archaea and bacteria). By one definition, plants form the clade Viridiplantae (Latin name for "green plants") which is sister of the Glaucophyta, and consists of the green algae and Embryophyta (land plants). The latter includes the flowering plants, conifers and other gymnosperms, ferns and their allies, hornworts, liverworts, and mosses. Most plants are multicellular organisms. Green plants obtain most of their energy from sunlight via photosynthesis by primary chloroplasts that are derived from endosymbiosis with cyanobacteria. Their chloroplasts contain chlorophylls a and b, which gives them their green color. Some plants are parasitic or mycotrophic and have lost the ability ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Calmodulin
Calmodulin (CaM) (an abbreviation for calcium-modulated protein) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. It is an intracellular target of the secondary messenger Ca2+, and the binding of Ca2+ is required for the activation of calmodulin. Once bound to Ca2+, calmodulin acts as part of a calcium signal transduction pathway by modifying its interactions with various target proteins such as kinases or phosphatases. Structure Calmodulin is a small, highly conserved protein that is 148 amino acids long (16.7 kDa). The protein has two approximately symmetrical globular domains (the N- and C- domains) each containing a pair of EF hand motifs separated by a flexible linker region for a total of four Ca2+ binding sites, two in each globular domain. In the Ca2+-free state, the helices that form the four EF-hands are collapsed in a compact orientation, and the central linker is disordered; in the Ca2+-saturated state, th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pathogen-associated Molecular Pattern
Pathogen-associated molecular patterns (PAMPs) are small molecular motifs conserved within a class of microbes. They are recognized by toll-like receptors (TLRs) and other pattern recognition receptors (PRRs) in both plants and animals. A vast array of different types of molecules can serve as PAMPs, including glycans and glycoconjugates. PAMPs activate innate immune responses, protecting the host from infection, by identifying some conserved nonself molecules. Bacterial lipopolysaccharides (LPSs), endotoxins found on the cell membranes of gram-negative bacteria, are considered to be the prototypical class of PAMPs. LPSs are specifically recognised by TLR4, a recognition receptor of the innate immune system. Other PAMPs include bacterial flagellin (recognized by TLR5), lipoteichoic acid from gram-positive bacteria (recognized by TLR2), peptidoglycan (recognized by TLR2), and nucleic acid variants normally associated with viruses, such as double-stranded RNA (dsRNA), recognized by ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ACP6
Lysophosphatidic acid phosphatase type 6 is an acid phosphatase enzyme that is encoded in humans by the ''ACP6'' gene. It acts as a phosphomonoesterase at low pHs. It is responsible for the hydrolysis of Lysophosphatidic acids (LPAs) to their respective monoacylglycerols and the release a free phosphate group in the process. The enzyme has higher activity for myristate-LPA (14 carbon chain), oleate-LPA (18 carbon chain and one unsaturated carbon-carbon bond), laurate-LPA (12 carbon chain) or palmitate-LPA (16 carbon chain). When the substrate is stearate-LPA (18 carbon chain), the enzyme has reduced activity. Phosphatidic acids can also be hydrolyzed by lysophosphatidic acid phosphatase, but at a significantly lower rate. The addition of the second fatty chain makes fitting into the active site much harder. LPAs are necessary for healthy cell growth, survival and pro-angiogenic factors for both in vivo and in vitro cells. Unbalanced concentrations of lysophosphatidic acid ph ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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