TPP1 is a member of the sedolisin family of serine proteases. The proenzyme is activated in the lysosome by auto-proteolysis where it cleaves tripeptides from the N-termini of substrates. Mutations of TPP1 are associated with late-infantile neuronal ceroid lipofuscinosis and Spinocerebellar Ataxia, Autosomal Recessive 7.

TPP1 is a member of the sedolisin family of serine proteases. The proenzyme is activated in the lysosome by auto-proteolysis where it cleaves tripeptides from the N-termini of substrates. Mutations of TPP1 are associated with late-infantile neuronal ceroid lipofuscinosis and Spinocerebellar Ataxia, Autosomal Recessive 7.

Sortilin was originally purified from human brain tissue and was identified as a new lipoprotein receptor, which was later identified as a multifunctional sorting receptor of the VPS10P-domain receptor family. Although Sortilin is predominately expressed in neurons of the central and the peripheral nervous systems, it is also expressed in metabolic tissues including liver. Sortilin functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Sortilin is critical for lipid metabolism, and it has been implicated in lipid disorders. Sortilin is also an APOE receptor implicated in Alzheimer disease.

Sortilin was originally purified from human brain tissue and was identified as a new lipoprotein receptor, which was later identified as a multifunctional sorting receptor of the VPS10P-domain receptor family. Although Sortilin is predominately expressed in neurons of the central and the peripheral nervous systems, it is also expressed in metabolic tissues including liver. Sortilin functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Sortilin is critical for lipid metabolism, and it has been implicated in lipid disorders. Sortilin is also an APOE receptor implicated in Alzheimer disease.

The autophagy-lysosomal pathway is involved in the degradation of long-lived proteins. The transcription factor EB (TFEB) plays a critical role in regulating basic cellular processes, such as lysosomal biogenesis and autophagy. The subcellular localization and activity of TFEB are regulated by mechanistic target of rapamycin (mTOR)-mediated phosphorylation. TFEB is also involved in physiological processes, and it induces the intracellular clearance of pathogenic factors in a variety of diseases, such as Parkinson's and Alzheimer's, suggesting that novel therapeutic strategies could be based on the modulation of TFEB activity.

The autophagy-lysosomal pathway is involved in the degradation of long-lived proteins. The transcription factor EB (TFEB) plays a critical role in regulating basic cellular processes, such as lysosomal biogenesis and autophagy. The subcellular localization and activity of TFEB are regulated by mechanistic target of rapamycin (mTOR)-mediated phosphorylation. TFEB is also involved in physiological processes, and it induces the intracellular clearance of pathogenic factors in a variety of diseases, such as Parkinson's and Alzheimer's, suggesting that novel therapeutic strategies could be based on the modulation of TFEB activity.

The autophagy-lysosomal pathway is involved in the degradation of long-lived proteins. The transcription factor EB (TFEB) plays a critical role in regulating basic cellular processes, such as lysosomal biogenesis and autophagy. The subcellular localization and activity of TFEB are regulated by mechanistic target of rapamycin (mTOR)-mediated phosphorylation. TFEB is also involved in physiological processes, and it induces the intracellular clearance of pathogenic factors in a variety of diseases, such as Parkinson's and Alzheimer's, suggesting that novel therapeutic strategies could be based on the modulation of TFEB activity.

The autophagy-lysosomal pathway is involved in the degradation of long-lived proteins. The transcription factor EB (TFEB) plays a critical role in regulating basic cellular processes, such as lysosomal biogenesis and autophagy. The subcellular localization and activity of TFEB are regulated by mechanistic target of rapamycin (mTOR)-mediated phosphorylation. TFEB is also involved in physiological processes, and it induces the intracellular clearance of pathogenic factors in a variety of diseases, such as Parkinson's and Alzheimer's, suggesting that novel therapeutic strategies could be based on the modulation of TFEB activity.

SHANK proteins are adapter proteins that are mainly localized to the post-synaptic densities of excitatory synapses. SHANK interacts with other post-synaptic density proteins such as PSD-95 and Homer to form a complex structure, which anchors glutamate receptors to the post-synaptic membrane.

SHANK proteins are adapter proteins that are mainly localized to the post-synaptic densities of excitatory synapses. SHANK interacts with other post-synaptic density proteins such as PSD-95 and Homer to form a complex structure, which anchors glutamate receptors to the post-synaptic membrane.

SynDIG1 is a type II transmembrane protein, which has been reported to regulate synaptic AMPA receptor content in rat hippocampal neurons in an activity-dependent manner. It has been found to be co-localized with AMPA receptors at both post-synaptic terminals and extra-synaptic regions.

SynDIG1 is a type II transmembrane protein, which has been reported to regulate synaptic AMPA receptor content in rat hippocampal neurons in an activity-dependent manner. It has been found to be co-localized with AMPA receptors at both post-synaptic terminals and extra-synaptic regions.

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.

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 hyper-phosphorylation, 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 hyper-phosphorylation, 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.