Disease relevance of NMT2

• Our findings provide the first evidence of higher expression of NMT2 in human colorectal adenocarcinomas and the interaction of both forms of NMT with various signaling molecules [1].
• To investigate whether NMT2 contributes to the pathogenesis of colorectal carcinoma, we observed a higher expression of NMT2 in most of the cases of cancerous tissues compared to normal tissues (84.6% of cases; P < 0.05) by Western blot analysis [1].
• In this review, we summarize the recent findings on NMT2 in human colon cancer in our laboratory [2].
• We also examined two other proteins that bear an N-terminal myristoylation signal, human immunodeficiency virus type 1 Gag and Hck protein tyrosine kinase, and found that Gag bound preferentially the NMT-2 isoform, while Hck bound mostly to NMT-1 [3].

High impact information on NMT2

• Western analysis revealed that while hNMT-2 appeared as a single 65-kDa protein in transfected COS-7 cells, hNMT-1 was processed to provide four distinct protein isoforms ranging from 49 to 68 kDa in size [4].
• Two NMT isoforms (NMT-1 and NMT-2) are expressed in mammalian cells [3].
• N-myristoyltransferase 2 expression in human colon cancer: cross-talk between the calpain and caspase system [1].
• Overall, the data indicate that NMT1 and NMT2 have only partially overlapping functions and that NMT1 is critical for tumor cell proliferation [5].

Physical interactions of NMT2

• Furthermore, protein-protein interaction of NMTs revealed that m-calpain interacts with NMT1 while caspase-3 interacts with NMT2 [2].

References