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The production of lysosomal proteins suggests one method of lysosome sustainment. Lysosomal protein genes are transcribed in the nucleus in a process that is controlled by transcription factor EB . [14] mRNA transcripts exit the nucleus into the cytosol, where they are translated by ribosomes.
Lysosomal-associated membrane protein 1 (LAMP-1) also known as lysosome-associated membrane glycoprotein 1 and CD107a (Cluster of Differentiation 107a), is a protein that in humans is encoded by the LAMP1 gene. The human LAMP1 gene is located on the long arm (q) of chromosome 13 at region 3, band 4 (13q34).
Structurally, the lamp proteins consist of two internally homologous lysosome-luminal domains separated by a proline-rich hinge region; at the C-terminal extremity there is a transmembrane region (TM) followed by a very short cytoplasmic tail (C). In each of the duplicated domains, there are two conserved disulfide bonds. This structure is ...
Its protein, LAMP2, is one of the lysosome-associated membrane glycoproteins. The protein encoded by this gene is a member of a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands. It may play a role in tumor cell metastasis. It may also function in the protection, maintenance, and adhesion of the ...
LAMP3 also known as DC-LAMP (Dendritic cell lysosomal associated membrane glycoprotein) is a member of the LAMP family along with LAMP1 and LAMP2, these proteins make up the members of the glycoconjugate coat present on the inside of the lysosomal membrane. [7] In humans, this protein is almost exclusively found in mature Dendritic cells. While ...
The protein encoded by this gene is a type III glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes. Studies of the similar proteins in mice and rat suggested that this protein may participate in membrane transportation and the reorganization of endosomal/lysosomal compartment. [13]
TMEM106B is composed of 274 amino acids and it has a molecular weight of 31 kDa. [10] It is found in the membrane of a lysosome (transmembrane protein) and has its highest expression in the central nervous system, specifically within neurons and oligodendrocytes. [12]
β-Glucocerebrosidase is maximally active at pH 5.5, the pH of the lysosomal compartment. [10] Within the lysosome it remains associated with the membrane, where it binds and degrades its substrate glucocerebroside (GluCer). It requires the activating protein Saposin C as well as negatively charged lipids for maximal catalytic activity.
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