The MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase mu
(2004) In Journal of Biological Chemistry 279(26). p.26922-26931- Abstract
- The MAM (meprin/A5-protein/PTPmu) domain is present in numerous proteins with diverse functions. PTPmu belongs to the MAM-containing subclass of protein-tyrosine phosphatases (PTP) able to promote cell-to-cell adhesion. Here we provide experimental evidence that the MAM domain is a homophilic binding site of PTPmu. We demonstrate that the MAM domain forms oligomers in solution and binds to the PTPmu ectodomain at the cell surface. The presence of two disulfide bridges in the MAM molecule was evidenced and their integrity was found to be essential for MAM homophilic interaction. Our data also indicate that PTPmu ectodomain forms oligomers and mediates the cellular adhesion, even in the absence of MAM domain homophilic binding. Reciprocally,... (More)
- The MAM (meprin/A5-protein/PTPmu) domain is present in numerous proteins with diverse functions. PTPmu belongs to the MAM-containing subclass of protein-tyrosine phosphatases (PTP) able to promote cell-to-cell adhesion. Here we provide experimental evidence that the MAM domain is a homophilic binding site of PTPmu. We demonstrate that the MAM domain forms oligomers in solution and binds to the PTPmu ectodomain at the cell surface. The presence of two disulfide bridges in the MAM molecule was evidenced and their integrity was found to be essential for MAM homophilic interaction. Our data also indicate that PTPmu ectodomain forms oligomers and mediates the cellular adhesion, even in the absence of MAM domain homophilic binding. Reciprocally, MAM is able to interact homophilically in the absence of ectodomain trans binding. The MAM domain therefore contains independent cis and trans interaction sites and we predict that its main role is to promote lateral dimerization of PTPmu at the cell surface. This finding contributes to the understanding of the signal transduction mechanism in MAM-containing PTPs. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1131162
- author
- Cismasiu, Valeriu LU ; Denes, Stefan A ; Reilander, Helmut ; Michel, Hartmut and Szedlacsek, Stefan E
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 279
- issue
- 26
- pages
- 26922 - 26931
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:15084579
- scopus:3042595911
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M313115200
- language
- English
- LU publication?
- no
- id
- 35768ced-84fc-4943-ac4f-a3a50a995dcb (old id 1131162)
- date added to LUP
- 2016-04-01 11:51:02
- date last changed
- 2022-01-26 19:09:07
@article{35768ced-84fc-4943-ac4f-a3a50a995dcb, abstract = {{The MAM (meprin/A5-protein/PTPmu) domain is present in numerous proteins with diverse functions. PTPmu belongs to the MAM-containing subclass of protein-tyrosine phosphatases (PTP) able to promote cell-to-cell adhesion. Here we provide experimental evidence that the MAM domain is a homophilic binding site of PTPmu. We demonstrate that the MAM domain forms oligomers in solution and binds to the PTPmu ectodomain at the cell surface. The presence of two disulfide bridges in the MAM molecule was evidenced and their integrity was found to be essential for MAM homophilic interaction. Our data also indicate that PTPmu ectodomain forms oligomers and mediates the cellular adhesion, even in the absence of MAM domain homophilic binding. Reciprocally, MAM is able to interact homophilically in the absence of ectodomain trans binding. The MAM domain therefore contains independent cis and trans interaction sites and we predict that its main role is to promote lateral dimerization of PTPmu at the cell surface. This finding contributes to the understanding of the signal transduction mechanism in MAM-containing PTPs.}}, author = {{Cismasiu, Valeriu and Denes, Stefan A and Reilander, Helmut and Michel, Hartmut and Szedlacsek, Stefan E}}, issn = {{1083-351X}}, language = {{eng}}, number = {{26}}, pages = {{26922--26931}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{The MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase mu}}, url = {{http://dx.doi.org/10.1074/jbc.M313115200}}, doi = {{10.1074/jbc.M313115200}}, volume = {{279}}, year = {{2004}}, }