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A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum

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Cominelli, Antoine [UCL] Halbout, Mathias [UCL] N'Kuli, Francisca [UCL] Lemoine, Pascale [UCL] Courtoy, Pierre J. [UCL] Marbaix, Etienne [UCL] Tyteca, Donatienne [UCL] Henriet, Patrick [UCL]

Matrix metalloproteinase-27 (MMP-27) is poorly characterized. Sequence comparison suggests that a C-terminal extension (CTE) includes a potential transmembrane domain as in some membrane-type (MT)-MMPs. Having noticed that MMP-27 was barely secreted, we investigated its subcellular localization and addressed CTE contribution for MMP-27 retention. Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC). Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted. CTE addition to rMMP-10 (a secreted MMP) caused ER retention and blocked secretion. Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14 led to effective phosphorylation upon forskolin stimulation, but not for MMP-27, excluding transmembrane anchorage. Moreover, MMP-27 was protected from digestion by proteinase K digestion. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein. In conclusion, MMP-27 is efficiently retained within the ER due to its unique C-terminal extension, which does not lead to stable membrane insertion. This could represent a novel ER retention system.

Document type Article de périodique (Journal article) – Article de recherche
Access type Accès restreint
Publication date 2014
Language Anglais
Journal information "Traffic" - Vol. 15, no. 4, p. 401-417 (2014)
Peer reviewed yes
Publisher Wiley ((United Kingdom) Oxford)
issn 1398-9219
e-issn 1600-0854
Publication status Publié
Affiliations UCL - SSS/DDUV - Institut de Duve
UCL - (SLuc) Service d'anatomie pathologique
Links
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Bibliographic reference Cominelli, Antoine ; Halbout, Mathias ; N'Kuli, Francisca ; Lemoine, Pascale ; Courtoy, Pierre J. ; et. al. A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum. In: Traffic, Vol. 15, no. 4, p. 401-417 (2014)
Permanent URL http://hdl.handle.net/2078.1/138323