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Beschreibung:
Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.
Beschreibung:
Glutathione S-transferases (GSTs) function to conjugate reduced glutathione to many exogenous and endogenous hydrophobic electrophiles. Although it shares the carboxy and amino-terminal glutathione S-transferase domains, GDAP1 is characterized as a GST-like protein because it contains an extended GST domain II and a predicted transmembrane domain, two characteristics which are unusual for GST family members. GDAP1 may function in a signal transduction pathway that is responsible for ganglioside-induced neurite differentiation and also may play a role in protecting myelin membranes from free-radical damage. Mutations in the gene encoding GDAP1 is the cause of many forms of Charcot-Marie-Tooth disease, a common inherited disorder of the peripheral nervous system that is characterized by reduced nerve conduction velocities, slow progressive distal muscle atrophy and absent deep tendon reflexes.
Beschreibung:
Glutathione S-transferases (GSTs) function to conjugate reduced glutathione to many exogenous and endogenous hydrophobic electrophiles. Although it shares the carboxy and amino-terminal glutathione S-transferase domains, GDAP1 is characterised as a GST-like protein because it contains an extended GST domain II and a predicted transmembrane domain, two characteristics which are unusual for GST family members. GDAP1 may function in a signal transduction pathway that is responsible for ganglioside-induced neurite differentiation and also may play a role in protecting myelin membranes from free-radical damage. Mutations in the gene encoding GDAP1 is the cause of many forms of Charcot-Marie-Tooth disease, a common inherited disorder of the peripheral nervous system that is characterised by reduced nerve conduction velocities, slow progressive distal muscle atrophy and absent deep tendon reflexes.
Beschreibung:
The Ras p21 family of guanine nucleotide proteins has been widely studied in view of its apparent role in signal transduction pathways and high frequency of mutations in human malignancies. It is now clear, however, that the Ras proteins (H-, K- and N-Ras p21) are members of a much larger superfamily of related proteins. Six members of this family, Rap 1A, Rap 1B, Rap 2, R-Ras, Ral A and Ral B, exhibit approximately 50% amino acid homology to Ras. The six mammalian Rho proteins (Rho A, B, C, G, 7 and 8) are approximately 30% homologous to Ras and are expressed in a wide range of cell types. Both Ras p21 and Rho p21, as well as other members of the Ras superfamily, contain a carboxy-terminal CAAX sequence (C, cysteine; A, aliphatic amino acid; X, any amino acid) which in the case of Ras has been shown to be essential for correct localization and function.
Beschreibung:
Vinexin is a 671 amino acid protein that is expressed as two isoforms, designated Vinexin alpha and Vinexin beta. Localized to cell junctions in both the cytoplasm and the cytoskeleton, Vinexin alpha functions to promote Actin stress fiber formation, playing an important role in modification of the Actin cytoskeleton. Like Vinexin alpha, Vinexin beta is localized to cell junctions in the cytoplasm, but is also found in the nucleus where it plays an important role in cell spreading and in activation of the JNK pathway in response to EGF stimulation. Although Vinexin alpha and Vinexin beta have different roles within the cell, both proteins contain three SH3 domains in their carboxy terminus and are expressed in a variety of tissues, including placenta, heart, liver, brain, pancreas and skeletal muscle. Together, Vinexin alpha and Vinexin beta are involved in cell-cell adhesion, signal transduction and cytoskeletal organization throughout the cell.
Beschreibung:
Lipin 1 is a member of the Lipin family of nuclear proteins. This family contains three members: Lipin 1, Lipin 2 and Lipin 3, all of which contain a nuclear signal sequence, a highly conserved amino-terminal (NLIP) domain and a carboxy-terminal (CLIP) domain. LPIN1 (Lipin 1) is crucial for normal adipose tissue development and metabolism. LPIN1 selectively activates a subset of PGC1 alpha target pathways, including fatty acid oxidation and mitochondrial oxidative phosphorylation by inducing expression of the nuclear receptor PPARalpha. LPIN1 also inactivates the lipogenic program and suppresses circulating lipid levels. An abundance of LPIN1 promotes fat accumulation and insulin sensitivity, whereas a deficiency in LPIN1 may deter normal adipose tissue development, resulting in insulin resistance and lipodystrophy, a heterogeneous group of disorders characterized by loss of body fat, fatty liver, hypertriglyceridemia and insulin resistance.
Beschreibung:
Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (1–3). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (1–3). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).
Beschreibung:
The Ras p21 family of guanine nucleotide proteins has been widely studied in view of its apparent role in signal transduction pathways and high frequency of mutations in human malignancies. It is now clear, however, that the Ras proteins (H-, K- and N-Ras p21) are members of a much larger superfamily of related proteins. Six members of this family, Rap 1A, Rap 1B, Rap 2, R-Ras, Ral A and Ral B, exhibit approximately 50% amino acid homology to Ras. The six mammalian Rho proteins (Rho A, B, C, G, 7 and 8) are approximately 30% homologous to Ras and are expressed in a wide range of cell types. Both Ras p21 and Rho p21, as well as other members of the Ras superfamily, contain a carboxy-terminal CAAX sequence (C, cysteine; A, aliphatic amino acid; X, any amino acid) which in the case of Ras has been shown to be essential for correct localization and function.
Beschreibung:
Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (1–3). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (1–3). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).
Beschreibung:
Gigaxonin, also referred to as giant axonal neuropathy, GAN1, or KLHL16, controls protein degradation and is essential for neuronal function and survival. Gigaxonin is a member of the cytoskeletal BTB/kelch repeat family and influences cytoskeletal organization and dynamics, playing a large role in neurofilament architecture. The amino terminal BTB domain of gigaxonin binds to the ubiquitin-activating enzyme E1, while the carboxy-terminal kelch repeat domain interacts directly with the light chain of microtubule-associated protein 1B (MAP1B), and tags it for degradation. Overexpression of MAP1B may lead to neuronal cell death, whereas a reduction of MAP1B significantly improves the survival rate of neurons. Mutations in the Gigaxonin gene result in human giant axonal neuropathy (GAN), an autosomal recessive neurodegenerative disorder characterised by axonal degeneration caused by cytoskeletal abnormalities, including accumulated intermediate filaments.
Beschreibung:
Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (13). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (13). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).
Beschreibung:
Tumor necrosis factor (TNF) is a pleiotropic cytokine whose function is mediated through two distinct cell surface receptors (1,2). These receptors, designated TNF-R1 and TNF-R2, are expressed on most cell types (1,3). The majority of TNF functions are primarily mediated through TNF-R1 (1,4). FAN (for factor associated with neutral sphingomyelinase (N-SMase) activation) is an intermediate protein that interacts with TNF-R1 to initiate TNF signaling events. FAN binds to TNF-R1 at the cytoplasmic NSD (N-SMase activating domain), which results in the initiation of the N-SMase pathway (5). N-SMase has been shown to be involved in TNF-induced Raf-1 activation (6). FAN contains four carboxy-terminal WD-repeat domains which appear to be involved in protein-protein interaction. The FAN WD-repeats may mediate the interaction between FAN and TNF-R1 (5).
Beschreibung:
Estrogen and progesterone receptor are members of a family of transcription factors that are regulated by the binding of their cognate ligands. The interaction of hormone-bound estrogen receptors with estrogen responsive elements(EREs) alters transcription of ERE-containing genes. The carboxy terminal region of the estrgen receptor contains the ligand binding domain, the amino terminus serves as the transactivation domain, and the DNA binding domain is centrally located. Two forms of estrogen receptor have been identified, ER Alpha and ER Beta. ER Alpha and ER Beta have been shown to be differentially activated by various ligands. The biological response to progesterone is mediated by two distinct forms of the human progesterone receptor (hPR-A and hPR-B), which arise from alternative splicing. In most cells, hPR-B functions as a transcriptional activator of progesterone-responsive gene, whereas hPR-A function as a transcriptional inhibitor of all steroid hormone receptors.
Beschreibung:
Vinexin is a 671 amino acid protein that is expressed as two isoforms, designated Vinexin alpha and Vinexin beta. Localized to cell junctions in both the cytoplasm and the cytoskeleton, Vinexin alpha functions to promote Actin stress fiber formation, playing an important role in modification of the Actin cytoskeleton. Like Vinexin alpha, Vinexin beta is localized to cell junctions in the cytoplasm, but is also found in the nucleus where it plays an important role in cell spreading and in activation of the JNK pathway in response to EGF stimulation. Although Vinexin alpha and Vinexin beta have different roles within the cell, both proteins contain three SH3 domains in their carboxy terminus and are expressed in a variety of tissues, including placenta, heart, liver, brain, pancreas and skeletal muscle. Together, Vinexin alpha and Vinexin beta are involved in cell-cell adhesion, signal transduction and cytoskeletal organization throughout the cell.
Beschreibung:
Tumor necrosis factor (TNF) is a pleiotropic cytokine whose function is mediated through two distinct cell surface receptors (1,2). These receptors, designated TNF-R1 and TNF-R2, are expressed on most cell types (1,3). The majority of TNF functions are primarily mediated through TNF-R1 (1,4). FAN (for factor associated with neutral sphingomyelinase (N-SMase) activation) is an intermediate protein that interacts with TNF-R1 to initiate TNF signaling events. FAN binds to TNF-R1 at the cytoplasmic NSD (N-SMase activating domain), which results in the initiation of the N-SMase pathway (5). N-SMase has been shown to be involved in TNF-induced Raf-1 activation (6). FAN contains four carboxy-terminal WD-repeat domains which appear to be involved in protein-protein interaction. The FAN WD-repeats may mediate the interaction between FAN and TNF-R1 (5).
Beschreibung:
The Ras p21 family of guanine nucleotide proteins has been widely studied in view of its apparent role in signal transduction pathways and high frequency of mutations in human malignancies. It is now clear, however, that the Ras proteins (H-, K- and N-Ras p21) are members of a much larger superfamily of related proteins. Six members of this family, Rap 1A, Rap 1B, Rap 2, R-Ras, Ral A and Ral B, exhibit approximately 50% amino acid homology to Ras. The six mammalian Rho proteins (Rho A, B, C, G, 7 and 8) are approximately 30% homologous to Ras and are expressed in a wide range of cell types. Both Ras p21 and Rho p21, as well as other members of the Ras superfamily, contain a carboxy-terminal CAAX sequence (C, cysteine; A, aliphatic amino acid; X, any amino acid) which in the case of Ras has been shown to be essential for correct localisation and function.
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