19458085

pubmed:Citation

30

Increasing evidence suggests that the cytoplasmic tail of membrane type 1 matrix metalloproteinase (MT1-MMP) is subject to phosphorylation and that this modification may influence its enzymatic activity at the cell surface. In this study, phosphorylated MT1-MMP is detected using a phospho-specific antibody recognizing a protein kinase C consensus sequence (phospho-TXR), and a MT1-MMP tail peptide is phosphorylated by exogenous protein kinase C. To characterize the potential role of cytoplasmic residue Thr(567) in these processes, mutants that mimic a state of either constitutive (T567E) or defective phosphorylation (T567A) were expressed and analyzed for their functional effects on MT1-MMP activity and cellular behavior. Phospho-mimetic mutants of Thr(567) exhibit enhanced matrix invasion as well as more extensive growth within a three-dimensional type I collagen matrix. Together, these findings suggest that MT1-MMP surface action is regulated by phosphorylation at cytoplasmic tail residue Thr(567) and that this modification plays a critical role in processes that are linked to tumor progression.

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http://linkedlifedata.com/resource/pubmed/journal/2985121R

http://linkedlifedata.com/resource/pubmed/chemical/Collagen Type I, http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 14, http://linkedlifedata.com/resource/pubmed/chemical/Threonine

Jul

pubmed-author:LiuYueyingY, pubmed-author:MossNatalie MNM, pubmed-author:MunshiH GHG, pubmed-author:StackM SharonMS, pubmed-author:WuYi IYI

24

NLM

19791-9

pubmed-meshheading:19458085-Amino Acid Sequence, pubmed-meshheading:19458085-Animals, pubmed-meshheading:19458085-Breast Neoplasms, pubmed-meshheading:19458085-Carcinoma, pubmed-meshheading:19458085-Cell Line, Tumor, pubmed-meshheading:19458085-Cell Movement, pubmed-meshheading:19458085-Cell Proliferation, pubmed-meshheading:19458085-Collagen Type I, pubmed-meshheading:19458085-Cytoplasm, pubmed-meshheading:19458085-Humans, pubmed-meshheading:19458085-Matrix Metalloproteinase 14, pubmed-meshheading:19458085-Molecular Sequence Data, pubmed-meshheading:19458085-Phosphorylation, pubmed-meshheading:19458085-Point Mutation, pubmed-meshheading:19458085-Rats, pubmed-meshheading:19458085-Threonine

Modulation of the membrane type 1 matrix metalloproteinase cytoplasmic tail enhances tumor cell invasion and proliferation in three-dimensional collagen matrices.