proliferation. ALDOA likely regulates actin cytoskeleton remodeling through interacting with cytohesin-2 (ARNO) and Arf6. ALDOA is ubiquitously expressed in most tissues, though it is predominantly expressed in developing embryo and adult muscle. In lymphocytes, ALDOA is the predominant aldolase isoform. Within the cell, ALDOA typically localizes to the cytoplasm, but it can localize to the nucleus during DNA synthesis of the cell cycle S phase. This nuclear localization is regulated by the protein kinases AKT and p38. It is suggested that the nucleus serves as a reservoir for ALDOA in low glucose conditions. ALDOA has also been found in mitochondria. ALDOA is regulated by the energy metabolism substrates glucose, lactate, and glutamine. In human mast cells (MCs), ALDOA has been observed to undergo post-translational regulation by protein tyrosine nitration, which may alter its relative affinity for FBP and/or IP3. This change then affects IP3 and PLC signaling cascades in IgE-dependent responses. Clinical significance Aldolase A (ALDOA) is highly expressed in multiple cancers, including lung squamous cell carcinoma (LSCC), renal cancer, and hepatocellular carcinoma. It is proposed that ALDOA overexpression enhances glycolysis in these tumor cells, promoting their growth. In LSCC, its upregulation correlates with metastasis and poor prognosis, while its downregulation reduces tumor cell motility and tumorigenesis. Thus, ALDOA could be a potential LSCC biomarker and therapeutic drug target. Aldolase A deficiency is a rare, autosomal recessive disorder that is linked to hemolysis and accompanied by weakness, muscle pain, and myopathy. Interactive pathway map Interactions Aldolase A has been shown to interact with: PLD2, actin, GLUT4, phospholipase D2, light chain 8 of dynein, erythrocyte anion exchanger Band 3 protein, ryanodine receptor, Cytohesin-2, and V-ATPase (vacuolar-type H+-ATPase). See also ALDOB ALDOC Fructose-bisphosphate aldolase References Further reading External links http://pdbdev.sdsc.edu:48346/pdb/molecules/pdb50_5.html PDBe-KB provides an overview of all the structure information available in the PDB for Human Fructose-bisphosphate aldolase A Enzymes Glycolysis