MARVELD1 regulates integrin beta 1-mediated cell adhesion and actin organization via inhibiting its pre-mRNA processing

作者：Wang Shan; Hu Jianran; Yao Yuanfei; Shi Ming; Yue Lei; Han Fang; Zhang Hao; He Jie; Liu Shanshan; Li Yu^*

来源：International Journal of Biochemistry & Cell Biology, 2013, 45(11): 2679-2687.

DOI：10.1016/j.biocel.2013.09.006

• MARVELD1
• Integrin beta 1
• Actin organization
• Cell adhesion
• 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 beta 1 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 131 was affected by MARVELD1. Taken together, our studies demonstrate that MARVELD1 plays a role in pre-mRNA processing of integrin beta 1, and thereby regulates cell adhesion and cell motility. These studies provide a novel regulatory mechanism of cell-ECM adhesion by nuclear protein in cells.

• 出版日期2013-11
• 单位哈尔滨工业大学