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Literature summary for 3.4.24.63 extracted from

  • Schaeffler, H.; Li, W.; Helm, O.; Krueger, S.; Boeger, C.; Peters, F.; Roecken, C.; Sebens, S.; Lucius, R.; Becker-Pauly, C.; Arnold, P.
    The cancer-associated meprin beta variant G32R provides an additional activation site and promotes cancer cell invasion (2019), J. Cell Sci., 132, jes220665 .
    View publication on PubMed
Search for more literature for 3.4.24.63

Cloned(Commentary)

Cloned (Comment) Organism
gene MEP1B, recombinant expression of wild-type and mutant enzymes in HEK-293 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
D47A the mutation is localized in the pro-peptide of the protease, the mutant is transported to the cell surface and exhibit expression comparable with wild-type meprin beta Homo sapiens
G32R naturally occuring mutant, the mutation is localized in the pro-peptide of the protease and identified in endometrium cancer, the mutant is transported to the cell surface and exhibit expression comparable with wild-type meprin beta, the mutant is more active against a peptide substrate (meprin beta-specific peptide substrate that is linked to a fluorogenic group (MCA) at the N-terminus and a quencher (DPN) at the C-terminus) and the interleukin-6 receptor than wild-type meprin beta. The change to an arginine residue at position 32 represents an additional activation site used by furin-like proteases in the Golgi, which consequently leads to reduced shedding by ADAM17. The meprin beta G32R variant assesses cell proliferation, invasion through a collagen IV matrix, and outgrowth from tumor spheroids. Increased meprin beta G32R activity at the cell surface reduces cell proliferation, but increases cell invasion. The G32R meprin beta variant shows increased activity. Phenotype, overview Homo sapiens
G32R/R61S site-directed mutagenesis, the double mutant has two altered sites that can no longer be proteolytically cleaved and cannot be activated or shedded Homo sapiens
additional information the expression patterns and cellular localizations of the two amino acid exchange variants do not differ from that of wild-type meprin beta Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
 Homo sapiens 9986
-
extracellular
-
 Homo sapiens
-
-
additional information the extracellular metalloprotease meprin beta is expressed as a homodimer and is primarily membrane bound. Meprin beta can be released from the cell surface by its known sheddases ADAM10 and ADAM17. Shedding of meprin beta mutant G32R mediated by ADAM17 is impaired Homo sapiens
-
-
plasma membrane membrane-bound Homo sapiens 5886
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc metalloproteinase Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16820
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification proteolytic activation of pro-meprin beta at the cell surface, serine protease matriptase-2 (MT-2) is a membrane-bound activator of meprin beta. Shedding of meprin beta is mediated by endogenous ADAM10 or ADAM17. Shedding of meprin beta mutant G32R mediated by ADAM17 is impaired Homo sapiens

Subunits

Subunits Comment Organism
homodimer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
meprin beta
-
 Homo sapiens
metalloprotease meprin beta
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction the change to an arginine residue at position 32 represents an additional activation site used by furin-like proteases in the Golgi, which consequently leads to reduced shedding by ADAM17. The meprin beta G32R variant assesses cell proliferation, invasion through a collagen IV matrix, and outgrowth from tumor spheroids. Increased meprin beta G32R activity at the cell surface reduces cell proliferation, but increases cell invasion. The G32R meprin beta variant shows increased activity Homo sapiens
additional information the extracellular metalloprotease meprin beta is expressed as a homodimer and is primarily membrane bound. Meprin beta can be released from the cell surface by its known sheddases ADAM10 and ADAM17. Activation of pro-meprin beta at the cell surface prevents its shedding, thereby stabilizing its proteolytic activity at the plasma membrane Homo sapiens