ErbB4 is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. ErbB4 is expressed in normal skeletal muscle,heart, pituitary, brain and several breast carcinomas. ErbB4 ligands include the neuregulins, beta-cellulin and heparin-binding EGFlike growth factor (HBEGF). Monomeric ErbB4 binds its ligands with low affinity. Several ErbB4 isoforms exist. Two of these differ in the presence of juxtamembrane extracellular sequences which regulate the ability of TACE (TNFα converting enzyme) to proteolytically cleave ErbB4 from the cell surface. These isoforms exhibit tissuespecific expression. Another isoform lacks the phosphoinositide 3kinase activation sequence present in the ErbB4 cytoplasmic domain. ErbB4 appears to play important roles in neuronal development, development of the heart and cancer.
MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. ERK is a versatile protein kinase that regulates many cellular functions. Growing evidence suggests that extracellular signal-regulated protein kinase 1/2 (ERK1/2) plays a crucial role in promoting cell death in a variety of neuronal systems, including neurodegenerative diseases. It is believed that the magnitude and the duration of ERK1/2 activity determine its cellular function. Activation of ERK1/2 are implicated in the pathophysiology of spinal cord injury (SCI). ERK-2, also known as Mitogen-activated protein kinase 1 (MAPK1), is a member of the protein kinase superfamily and MAP kinase subfamily. MKP-3 is a dual specificity phosphatase exclusively specific to MAPK1 for its substrate recognition and dephosphorylating activity. The activation of MAPK1 requires its phosphorylation by upstream kinases. Upon activation, MAPK1 translocates to the nucleus of the stimulated cells, where it phosphorylates nuclear targets. MAPK1 is involved in both the initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors such as ELK1. MAPK1 acts as a transcriptional repressor which represses the expression of interferon gamma-induced genes.
ERK3; also known as MAPK12 and p38-gamma; belongs to theprotein kinase superfamily; CMGC Ser/Thr protein kinase family and MAP kinase subfamily. ERK3 is highly expressed in skeletal muscle and heart.ERK3 is a serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly; p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK12 is required for the normal kinetochore localization of PLK1; prevents chromosomal instability and supports mitotic cell viability. MAPK12-signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration.
Human Erythroid Membrane-Associated Protein (ERMAP) is a cell surface transmembrane protein that belongs to the immunoglobulin superfamily. It is hghly expressed in bone marrow and to a lower extent in leukocytes, thymus, lymph node and spleen. ERMAP contains 1 B30.2/SPRY domain and 1 Ig-like V-type (immunoglobulin-like) domain. It may serve as an erythroid cell receptor, possibly as a mediator of cell adhesion. ERMAP is responsible for the Scianna/Radin blood group system. Two transcript variants encoding the same protein have been found for this gene ERMAP.
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