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MT1-MMP Recruits the ER-Golgi SNARE Bet1 for Efficient MT1-MMP Transport to the Plasma Membrane

Overview
Journal J Cell Biol
Specialty Cell Biology
Date 2019 Sep 15
PMID 31519727
Citations 9
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Abstract

Metastasis is a major cause of cancer-related death. Membrane type 1-matrix metalloproteinase (MT1-MMP) is a critical protease for local invasion and metastasis. MT1-MMP is synthesized in the endoplasmic reticulum (ER) and transported in vesicles to invadopodia, specialized subdomains of the plasma membrane, through secretory and endocytic recycling pathways. The molecular mechanism underlying intracellular transport of MT1-MMP has been extensively studied, but is not fully understood. We show that MT1-MMP diverts the SNARE Bet1 from its function in ER-Golgi transport, to promote MT1-MMP trafficking to the cell surface, likely to invadopodia. In invasive cells, Bet1 is localized in MT1-MMP-positive endosomes in addition to the Golgi apparatus, and forms a novel SNARE complex with syntaxin 4 and endosomal SNAREs. MT1-MMP may also use Bet1 for its export from raft-like structures in the ER. Our results suggest the recruitment of Bet1 at an early stage after MT1-MMP expression promotes the exit of MT1-MMP from the ER and its efficient transport to invadopodia.

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References
1.
Tisdale E, Bourne J, Khosravi-Far R, Der C, Balch W . GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex. J Cell Biol. 1992; 119(4):749-61. PMC: 2289685. DOI: 10.1083/jcb.119.4.749. View

2.
Fukasawa M, Varlamov O, Eng W, Sollner T, Rothman J . Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation. Proc Natl Acad Sci U S A. 2004; 101(14):4815-20. PMC: 387331. DOI: 10.1073/pnas.0401183101. View

3.
Jacob A, Jing J, Lee J, Schedin P, Gilbert S, Peden A . Rab40b regulates trafficking of MMP2 and MMP9 during invadopodia formation and invasion of breast cancer cells. J Cell Sci. 2013; 126(Pt 20):4647-58. PMC: 3795337. DOI: 10.1242/jcs.126573. View

4.
Monteiro P, Rosse C, Castro-Castro A, Irondelle M, Lagoutte E, Paul-Gilloteaux P . Endosomal WASH and exocyst complexes control exocytosis of MT1-MMP at invadopodia. J Cell Biol. 2013; 203(6):1063-79. PMC: 3871436. DOI: 10.1083/jcb.201306162. View

5.
Jahn R, Scheller R . SNAREs--engines for membrane fusion. Nat Rev Mol Cell Biol. 2006; 7(9):631-43. DOI: 10.1038/nrm2002. View