Rab7, a small GTPase of the Rab family, plays multiple roles including vesicular transport, endocytic trafficking, and autophagy. Rab7 is associated with both the endosome and lysosome, and it facilitates endosomal maturation, transport from the late endosome to the lysosome, and positioning of the endosome and lysosome via regulating their movement along cytoskeleton. Consistently, mutations or dysfunctions of Rab7 result in traffic disorders, which cause various diseases, such as neuropathy, cancer and lipid metabolism disease. Rab7 also plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses.

Rab7, a small GTPase of the Rab family, plays multiple roles including vesicular transport, endocytic trafficking, and autophagy. Rab7 is associated with both the endosome and lysosome, and it facilitates endosomal maturation, transport from the late endosome to the lysosome, and positioning of the endosome and lysosome via regulating their movement along cytoskeleton. Consistently, mutations or dysfunctions of Rab7 result in traffic disorders, which cause various diseases, such as neuropathy, cancer and lipid metabolism disease. Rab7 also plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses.

Rab7, a small GTPase of the Rab family, plays multiple roles including vesicular transport, endocytic trafficking, and autophagy. Rab7 is associated with both the endosome and lysosome, and it facilitates endosomal maturation, transport from the late endosome to the lysosome, and positioning of the endosome and lysosome via regulating their movement along cytoskeleton. Consistently, mutations or dysfunctions of Rab7 result in traffic disorders, which cause various diseases, such as neuropathy, cancer and lipid metabolism disease. Rab7 also plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses.

Rab7, a small GTPase of the Rab family, plays multiple roles including vesicular transport, endocytic trafficking, and autophagy. Rab7 is associated with both the endosome and lysosome, and it facilitates endosomal maturation, transport from the late endosome to the lysosome, and positioning of the endosome and lysosome via regulating their movement along cytoskeleton. Consistently, mutations or dysfunctions of Rab7 result in traffic disorders, which cause various diseases, such as neuropathy, cancer and lipid metabolism disease. Rab7 also plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses.

Synaptosomal-associated protein 25 (SNAP-25) is a component of the trans-SNARE (t-SNARE) complex. SNAP-25 has been reported to account for the specificity of membrane fusion, and to directly execute fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together. SNAP-25 has been shown to inhibits both ATP-dependent and independent Ca2+-triggered release of glutamate from central nervous system (CNS) synaptosomal membranes. This indicates that SNAP-25 has a role not only in the formation of the synaptic vesicle-target v- and t-SNARE complex, but also in the final neurotransmitter release.

Synaptosomal-associated protein 25 (SNAP-25) is a component of the trans-SNARE (t-SNARE) complex. SNAP-25 has been reported to account for the specificity of membrane fusion, and to directly execute fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together. SNAP-25 has been shown to inhibits both ATP-dependent and independent Ca2+-triggered release of glutamate from central nervous system (CNS) synaptosomal membranes. This indicates that SNAP-25 has a role not only in the formation of the synaptic vesicle-target v- and t-SNARE complex, but also in the final neurotransmitter release.

Dopamine Receptor D4 (DRD4) is a G-protein coupled receptor which inhibits adenyl cyclase activity. It is linked to many neurological and psychiatric conditions including schizophrenia and bipolar disorder, addictive behaviors, Parkinson’s disease, and eating disorders such as anorexia nervosa. DRD4 mutations have been associated with various behavioral phenotypes, including autonomic nervous system dysfunction, attention deficit/hyperactivity disorder, and the personality trait of novelty seeking.

Dopamine Receptor D4 (DRD4) is a G-protein coupled receptor which inhibits adenyl cyclase activity. It is linked to many neurological and psychiatric conditions including schizophrenia and bipolar disorder, addictive behaviors, Parkinson’s disease, and eating disorders such as anorexia nervosa. DRD4 mutations have been associated with various behavioral phenotypes, including autonomic nervous system dysfunction, attention deficit/hyperactivity disorder, and the personality trait of novelty seeking.

The flotillin family is composed of two highly homologous proteins, flotillin-1 and flotillin-2 that share ~50% amino acid sequence similarity. Flotillins are ubiquitously expressed, membrane-associated proteins, and were shown to be associated with lipid microdomains called membrane rafts. Flotillins are present in various cellular compartments, including the plasma membrane and endosomes, and they have been suggested to function in cellular signaling and membrane trafficking processes, including endocytosis and endosomal trafficking.

The flotillin family is composed of two highly homologous proteins, flotillin-1 and flotillin-2 that share ~50% amino acid sequence similarity. Flotillins are ubiquitously expressed, membrane-associated proteins, and were shown to be associated with lipid microdomains called membrane rafts. Flotillins are present in various cellular compartments, including the plasma membrane and endosomes, and they have been suggested to function in cellular signaling and membrane trafficking processes, including endocytosis and endosomal trafficking.

The flotillin family is composed of two highly homologous proteins, flotillin-1 and flotillin-2 that share ~50% amino acid sequence similarity. Flotillins are ubiquitously expressed, membrane-associated proteins, and were shown to be associated with lipid microdomains called membrane rafts. Flotillins are present in various cellular compartments, including the plasma membrane and endosomes, and they have been suggested to function in cellular signaling and membrane trafficking processes, including endocytosis and endosomal trafficking.

The flotillin family is composed of two highly homologous proteins, flotillin-1 and flotillin-2 that share ~50% amino acid sequence similarity. Flotillins are ubiquitously expressed, membrane-associated proteins, and were shown to be associated with lipid microdomains called membrane rafts. Flotillins are present in various cellular compartments, including the plasma membrane and endosomes, and they have been suggested to function in cellular signaling and membrane trafficking processes, including endocytosis and endosomal trafficking.

Beclin-1 plays a central role in autophagy and is involved in autophagosome formation. It acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate. Beclin-1 is necessary for the initiation of autophagy, and it has been shown to be reduced in the brains of patients with Alzheimer’s disease. Reduced Beclin-1 levels lead to decreased autophagy, the accumulation of Aβ peptides, and neurodegeneration in mouse models of Alzheimer's disease.

Beclin-1 plays a central role in autophagy and is involved in autophagosome formation. It acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate. Beclin-1 is necessary for the initiation of autophagy, and it has been shown to be reduced in the brains of patients with Alzheimer’s disease. Reduced Beclin-1 levels lead to decreased autophagy, the accumulation of Aβ peptides, and neurodegeneration in mouse models of Alzheimer's disease.

Beclin-1 plays a central role in autophagy and is involved in autophagosome formation. It acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate. Beclin-1 is necessary for the initiation of autophagy, and it has been shown to be reduced in the brains of patients with Alzheimer’s disease. Reduced Beclin-1 levels lead to decreased autophagy, the accumulation of Aβ peptides, and neurodegeneration in mouse models of Alzheimer’s disease.

Beclin-1 plays a central role in autophagy and is involved in autophagosome formation. It acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate. Beclin-1 is necessary for the initiation of autophagy, and it has been shown to be reduced in the brains of patients with Alzheimer’s disease. Reduced Beclin-1 levels lead to decreased autophagy, the accumulation of Aβ peptides, and neurodegeneration in mouse models of Alzheimer’s disease.

Tau protein promotes microtubule assembly and stability. Tau is abundant in neurons of the central nervous system, and is expressed at low levels in astrocytes and oligodendrocytes. Abnormal hyperphosphorylation, aggregation, and toxic gain of function of tau is associated with several neurological disorders, including Alzheimer’s disease (AD). The major building block of neurofibrillary lesions in AD brains consists of paired helical filaments (PHFs) of abnormally hyperphosphorylated tau. Six isoforms of tau are generated by alternative splicing of the MAPT gene. These isoforms are distinguished by the number of tubulin binding domains, 3 (3R) or 4 (4R), in the C-terminal of the protein and by one (1N), two (2N), or no (0N) inserts in the N-terminal domain.  Tau isoforms are differentially expressed during development.

Tau protein promotes microtubule assembly and stability. Tau is abundant in neurons of the central nervous system, and is expressed at low levels in astrocytes and oligodendrocytes. Abnormal hyperphosphorylation, aggregation, and toxic gain of function of tau is associated with several neurological disorders, including Alzheimer’s disease (AD). The major building block of neurofibrillary lesions in AD brains consists of paired helical filaments (PHFs) of abnormally hyperphosphorylated tau. Six isoforms of tau are generated by alternative splicing of the MAPT gene. These isoforms are distinguished by the number of tubulin binding domains, 3 (3R) or 4 (4R), in the C-terminal of the protein and by one (1N), two (2N), or no (0N) inserts in the N-terminal domain.  Tau isoforms are differentially expressed during development.

Tau protein promotes microtubule assembly and stability. Tau is abundant in neurons of the central nervous system, and is expressed at low levels in astrocytes and oligodendrocytes. Abnormal hyperphosphorylation, aggregation, and toxic gain of function of tau is associated with several neurological disorders, including Alzheimer’s disease (AD). The major building block of neurofibrillary lesions in AD brains consists of paired helical filaments (PHFs) of abnormally hyperphosphorylated tau. Six isoforms of tau are generated by alternative splicing of the MAPT gene. These isoforms are distinguished by the number of tubulin binding domains, 3 (3R) or 4 (4R), in the C-terminal of the protein and by one (1N), two (2N), or no (0N) inserts in the N-terminal domain.  Tau isoforms are differentially expressed during development.

Tau protein promotes microtubule assembly and stability. Tau is abundant in neurons of the central nervous system, and is expressed at low levels in astrocytes and oligodendrocytes. Abnormal hyperphosphorylation, aggregation, and toxic gain of function of tau is associated with several neurological disorders, including Alzheimer’s disease (AD). The major building block of neurofibrillary lesions in AD brains consists of paired helical filaments (PHFs) of abnormally hyperphosphorylated tau. Six isoforms of tau are generated by alternative splicing of the MAPT gene. These isoforms are distinguished by the number of tubulin binding domains, 3 (3R) or 4 (4R), in the C-terminal of the protein and by one (1N), two (2N), or no (0N) inserts in the N-terminal domain.  Tau isoforms are differentially expressed during development.