MARVELD1 regulates integrin β1-mediated cell adhesion and actin organization via inhibiting its pre-mRNA processing.
Cell adhesion on an extracellular matrix (ECM) participates in cell motility, invasion, cell signal transduction and gene expression. Many nuclear proteins regulate cell-ECM adhesion through managing the transcription of cell adhesion-related genes. Here, we identified MARVEL [MAL (The myelin and lymphocyte protein) and related proteins for vesicle trafficking and membrane link] domain containing 1 (MARVELD1) that could suppress cell spreading and complicate actin organization. Over-expression of MARVELD1 in NIH3T3 cells decreased the expression level of integrin β1 and vinculin, and further led to dephosphorylation of focal adhesion kinase (FAK) at Tyr 397. We also found that MARVELD1 partially colocalized with serine/arginine-rich splicing factor 2 (SC35) and interacted with nuclear cap binding protein subunit 2 (CBP20). Finally, we demonstrated that pre-mRNA processing of integrin β1 was affected by MARVELD1. Taken together, our studies demonstrate that MARVELD1 plays a role in pre-mRNA processing of integrin β1, and thereby regulates cell adhesion and cell motility. These studies provide a novel regulatory mechanism of cell-ECM adhesion by nuclear protein in cells.
School of Life Science and Technology, Harbin Institute of Technology, Harbin 150001, China.
Shan
S
Wang
Jianran
J
Hu
Yuanfei
Y
Yao
Ming
M
Shi
Lei
L
Yue
Fang
F
Han
Hao
H
Zhang
Jie
J
He
Shanshan
S
Liu
Yu
Y
Li
D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000378:metabolism*; D000818:Animals; D002448:Cell Adhesion / Q000235:genetics; D002465:Cell Movement / Q000235:genetics; D016000:Cluster Analysis; D051416:Focal Adhesion Protein-Tyrosine Kinases / Q000378:metabolism; D022001:Focal Adhesions / Q000378:metabolism; D020869:Gene Expression Profiling; D017930:Genes, Reporter; D049452:Green Fluorescent Proteins / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D019012:Integrin beta1 / Q000235:genetics* / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D008954:Models, Biological; D041681:NIH 3T3 Cells; D039502:Nuclear Cap-Binding Protein Complex / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000378:metabolism; D012322:RNA Precursors / Q000235:genetics* / Q000378:metabolism; D012323:RNA Processing, Post-Transcriptional / Q000235:genetics*; D012261:Ribonucleoproteins / Q000378:metabolism; D000068103:Serine-Arginine Splicing Factors
D000199:Actins; D019012:Integrin beta1; C542435:MARVELD1 protein, human; D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D039502:Nuclear Cap-Binding Protein Complex; D009687:Nuclear Proteins; D012322:RNA Precursors; D012261:Ribonucleoproteins; C073288:SRSF2 protein, human; D049452:Green Fluorescent Proteins; D000068103:Serine-Arginine Splicing Factors; D019000:Phosphotyrosine; D051416:Focal Adhesion Protein-Tyrosine Kinases
Actin organization; Cell adhesion; Integrin β1; MARVELD1; Pre-mRNA processing