Table 1.

The molecular and biological functions associated with LIMA1.

Processes	The molecules that interacts with LIMA1	Biological significance	References
Actin dynamics	Arp2/3, ERK/MAPK, G-actin, MAL/MRTF, CDC14A, LUZP1, E-cadherin, α-catenin, β-catenin, F-actin, Vinculin, myosin Va	Stabilizing actin filament networks to control actin dynamics	(7, 12, 20–24, 26)
Cell adhesion and metastasis	PINCH-1, PDGF, paxillin, Rab40b-Cullin5, EGF, EPK signaling pathway, p53, DNp73, IGF1R-AKT/STAT3 signaling pathway	Regulation of adherens junctions and initiation of the invasion-metastasis cascade	(29–35)
EMT	EGF, DNp73, E-cadherin, β-catenin, Arp2/3, Slug, PI3K-AKT and JAK-STAT signaling pathway	Bidirectional regulation of the epithelial-to-mesenchymal transition	(32, 35, 38–45)
Epithelial defense against cancer	Cav-1, Myosin II, PKA, Rab5, paxillin	Promotion of apical extrusion in transformed cells	(21, 49–51)
Endothelial dynamics	VE-cadherin, α-catenin, β-catenin, ARP2/3, cLP, JAIL	Mediating the formation and maintenance of endothelial cell adherens junctions and integrity	(54–58)
Angiogenesis	ERK, miR-93-5p	Promotion of new angiogenesis during tumor development	(59, 60)
Inflammatory reaction	MiR-29a-3p, miR-29b-3p, miR-155-5p	Stimulation of inflammatory cytokines, leading to endothelial barrier dysfunction	(63)
Cell division	Arv1, supervillin, Myosin II, septin 2, small GTPases, RhoA	Cooperating to modulate actin and microtubule motor functions, drive the contraction of the cleavage furrow and maintain proper cell division	(66–68)
Membrane dynamics	Actin, β-catenin, p120, the naïve pluripotency transcription factors	Pluripotency control of membrane dynamics and cellular metabolism	(71)
Lipid metabolism	NPC1L1	Regulation of cholesterol transport and promotion of effective cholesterol absorption by the intestines	(75–77)