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MAD2L1-binding protein (MAD2L1) is a component of the mitotic spindle assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. MAD2L1 is vital for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate.

MAD2L1-binding protein (MAD2L1BP) is a member of the MAD2L1BP family.MAD2L1BP is a binding protein of the MAD2 mitotic arrest deficient-like 1 (MAD2/MAD2L1). MAD2 is a fundamental factor of the spindle checkpoint which delays the onset of anaphase until all the kinetochores are connected to the spindle. The MAD2L1BP protein acts to curb the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 once it dissociated from the MAD2L1-CDC20 complex. For the duration of the cell cycle, MAD2L1BP levels increase and then remain constant until late mitosis after which they drop.

SMAD2 is part of the SMAD family of proteins that mediate signal transduction by the TGF-beta/BMP-2/4 cytokine superfamily from receptor Ser/Thr protein kinases at the cell surface to the nucleus. Phosphorylated SMAD2 is then able to form a complex with SMAD4 or SARA. These complexes accumulate in the cell nucleus, where they are directly participating in the regulation of gene expression. SMAD2 mediates the signal of the TGF-beta, and therefore regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. SMAD2 is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein.
TGF-beta 1 acts on adjacent stromal cells to turn on SMAD2 signalling that could lead to stromal decidualization. SMAD2 is the downstream signal transducers of TGF-beta-1 in human dental pulp cells.