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Pathways

Signaling Pathways

Displaying 277 to 288 (of 537 pathways)

Dynamic regulation of the actin cytoskeleton underpins a multitude of cellular processes, from cell movement and polarization1,2 to cell division.3 The actin cytoskeleton and the proteins involved in its regulation are also fundamentally linked to endocytosis and membrane trafficking.4,5 Members of the Rho family of small GTPases have emerged as important overseers of the actin cytoskeleton and a number of Rho family members and their downstream effector proteins have been linked to specific actin pathways. Among the Rho family actin regulators is Cdc42 is a small GTPase responsible for a large number of eukaryotic cell signaling pathways(Ref.1).CDC42 acts downstream of cell surface receptors to regulate the formation of different F-actin-containing structures. It[..]

Ran is a member of the Ras family of small GTPases. The Ran subgroup is represented by its lone member, Ran, that is distinguished from Ras GTPases by its lipid modification and atypical subcellular localization. Unlike most other Ras-related proteins, Ran is not modified to bind to cell membranes. Instead, Ran protein is localized throughout the cell, where it is concentrated primarily in the nucleus (Ref.1). Ran is regulated by a cytosolic RanGAP1 (Ran GTPase–Activating Protein-1) and by a RanGEF (Chromatin-Bound Guanine Nucleotide Exchange Factor). The distribution of RanGTP provides important spatial information that directs cellular activities during different parts of the cell cycle. During interphase, the localization of RanGEF and RanGAP1 predicts that[..]

Our immune system is largely controlled by the action of pleiotropic cytokines and growth factors, small secreted proteins, which bind to receptors on the surface of immune cells to initiate an appropriate physiological response. The cellular response to cytokines and growth factors is predominantly executed by intracellular proteins known as the Janus kinases (JAKs) and the signal transducers and activators of transcriptions (STATs). These  kinases activated upon ligand binding causes the phosphorylation of tyrosine residues within the receptor intracellular region and phosphorylation of other signalling proteins recruited to the receptor complex like signal transducers and activators of transcriptions (STATs). Once phosphorylated, STATs translocate to the[..]

Calpain is an evolutionary old family of soluble, neutral, calcium-dependent proteases, which have the unique property of using protein cleavage to modify the activity/function of their substrate proteins. There are two major calpain isoforms in the brain, calpain-1 and calpain-2. Calpain-1 and Calpain-2 exhibit opposite functions in both synaptic plasticity and neurodegeneration. Calpain-1 activation is required for the induction of long-term potentiation (LTP) and is generally neuroprotective, while calpain-2 activation limits the extent of potentiation and is neurodegenerative. Calpains release the link between the integrin-dependent FA complex and the actin cytoskeleton by proteolysis of talin, which allows proper cell migration. The activity of Calpains is tightly[..]

Members of the TNFR (Tumor Necrosis Factor Receptor) superfamily are important for cell growth and survival. CD27 is a member of the TNFR superfamily, which includes TNFR types I and II, NGFR (Nerve Growth Factor Receptor), CD30 (associated with Hodgkin lymphoma), Fas/Apo1 (CD95), CD40, 4–1BB, and OX40. These receptors are known to play a very important role in cell growth and differentiation, as well as apoptosis or programmed cell death. In addition to providing costimulatory signals for cell proliferation, ligation of both TNFR1 and Fas can result in programmed cell death or apoptosis. The underlying mechanism requires an intact 80-aa stretch present in the cytoplasmic tails of both TNFR1 and Fas, termed the DD (Death Domain) (Ref.1). CD27 is a disulfide-linked[..]

PKR (Protein Kinase-R) is a 68-kDa serine–threonine kinase that appears to play a primary role in mediating the antiviral activities of infected cells. PKR mediates apoptosis induced by many different stimuli, such as LPS (Lipopolysaccharides), TNF-Alpha (Tumour Necrosis Factor-Alpha), viral infection, or serum starvation. Viral infection leads to the increased expression and secretion of the cytokine IFN-Gamma (Interferon- Gamma) from host cells. IFN-gamma induces the dsRNA (Double-Stranded RNA)-dependent PKR. dsRNA, produced during viral replication, is an active component of a viral infection that stimulates antiviral responses in infected cells (Ref.1). The PKR protein is enzymatically inactive unless it is activated by binding to dsRNA. PKR activates as a kinase[..]

Phosphatase and tensin homolog deleted from chromosome 10 (PTEN) is a tumor suppressor protein, that is linked to AKT signaling, critically controlling proliferation, survival, migration, energy metabolism and cellular architecture in hematopoietic cells. PTEN is a dual-specificity protein phosphatase and an inositol phospholipid phosphatase that dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PIP3), thus producing phosphatidylinositol 4,5-bisphosphate (PIP2) and thereby negatively regulating oncogenic and nononcogenic PI3K/AKT signaling. PTEN may have additional phosphatase-independent activities, as well as other functions in the nucleus (Ref.1 and 2). PTEN's tumor-suppressing function largely relies on the protein's phosphatase activity and subsequent[..]

Irradiation of DNA by UV (Ultraviolet light) causes lesions, such as Cyclobutane-Pyrimidine Dimers or 6-4PPs (6-4 Pyrimidine Pyrimidone). The most common covalently linked adjoining pyrimidines are T-T (Thymine dimers), T-C (Thymine-Cytosine dimers) and C-C (Cytosine-Cytosine dimers). T-T dimers cause kinks in the DNA strand that prevent both replication and transcription of that part of the DNA. Because they block DNA replication (and therefore prevent cells from reproducing), T-T dimers and other forms of UV damage cannot be inherited, and thus do not constitute mutations. Such kinds of DNA damage are known as premutational lesions because they prevent both transcription and replication of the genes in which they are present and these lesions are fatal if they go[..]

8-oxo-7,8-dihydroguanine (8-oxoG) is a pre-mutagenic DNA lesion that is formed by the oxidation of guanine. Reactive oxygen species (ROS) that is primarily responsible for the damage of guanine is produced as a result of several endogenous processes or environmental agents. ROS can cause damage to cellular macromolecules like proteins, lipids and nucleic acids. Proteins, proteins, lipids and RNA having oxidative damage are generally degraded and recycled, whereas DNA lesions like 8-oxoG need to be repaired to maintain genomic integrity (Ref.1 and 2). 8-oxoG is generally repaired in human through base excision repair (BER) pathway. The enzyme human 8-oxoG DNA glycosylase 1 (HOGG1) is the primary enzyme that initiates the repair of 8-oxoG. OGG1 initiated BER[..]

An effective immune response depends on the ability of specialized immunocytes to identify foreign molecules and respond by differentiation into mature effector cells. A cell-surface antigen recognition apparatus and a complex intracellular receptor-coupled signal-transducing machinery mediate this tightly regulated process, which operate at high fidelity to discriminate self from nonself antigens. Activation of T-Cell requires sustained physical interaction of the TCR (T-Cell Receptor) with a MHC (Major Histocompatibility Complex)–presented peptide antigen that results in a temporal and spatial reorganization of multiple cellular elements at the T-Cell–Antigen Presenting Cell contact region, a specialized region referred to as the IS (Immunological[..]

CD40, a TNFR (Tumor Necrosis Factor Receptor) family member, conveys signals regulating diverse cellular responses, ranging from proliferation and differentiation to growth suppression and cell death. First identified and functionally characterized on B-Cells, CD40 is expressed on a plethora of different cell types, including B-Cells, macrophages, dendritic cells, endothelial cells, and fibroblasts, and this widespread expression accounts for the central role of CD40 in the regulation of immune response and host defense (Ref.1). Binding of CD40 with its counter receptor, CD154 (also termed CD40L [CD40 ligand] or GP39), acts on Antigen presenting cells and T-Cells in a bi-directional fashion, mediating both humoral and cellular immune responses (Ref.2). Unique to[..]

Eukaryotic transcription is a highly regulated process, and acetylation plays a major role in this regulation. Acetylation can occur on histones, DNA-binding TF (Transcription Factors), acetylases, nuclear import factors, non-nuclear proteins (Alpha-tubulin) and proteins that shuttle from the nucleus to the cytoplasm, such as the Importin-Alpha family of nuclear import factors. Acetylation can modify the recognition of DNA, the stability of proteins and the interaction between proteins. They regulate different cellular processes, such as microtubule function or nuclear import (Ref.1). By modifying chromatin proteins and transcription-related factors, these acetylases regulate diverse functions, including DNA recognition, protein-protein interaction, protein stability,[..]

Displaying 277 to 288 (of 537 pathways)
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