Abstract
Regenerative medicine represented by stem cell technology has become one of the pillar medical technologies for human disease treatment. Cytoskeleton plays important roles in maintaining cell morphology, bearing external forces, and maintaining the effectiveness of cell internal structure, among which cytoskeleton related proteins are involved in and play an indispensable role in the changes of cytoskeleton. PDLIM5 is a cytoskeleton-related protein that, like other cytoskeletal proteins, acts as a binding protein. PDZ and LIM domain 5 (PDLIM5), also known as ENH (Enigma homolog), is a cytoplasmic protein with a molecular mass of about 63 KDa that consists of a PDZ domain at the N-terminus and three LIM domains at the C-terminus. PDLIM5 binds to the cytoskeleton and membrane proteins through its PDZ domain and interacts with various signaling molecules, including protein kinases and transcription factors, through its LIM domain. As a cytoskeleton-related protein, PDLIM5 plays an important role in regulating cell proliferation, differentiation and cell fate decision in multiple tissues and cell types. In this review, we briefly summarize the state of knowledge on the PDLIM5 gene, structural properties, and molecular functional mechanisms of the PDLIM5 protein, and its role in cells, tissues, and organ systems, and describe the possible underlying molecular signaling pathways. In the last part of this review, we will focus on discussing the limitations of existing research and the future prospects of PDLIM5 research in turn.
Highlights
PDZ and LIM domain 5 is a cytoskeleton-related protein that was first discovered by Kuroda et al (1996), using yeast two-hybrid technology with protein kinase C (PKC) as the bait protein
The cross-linking with actin cytoskeleton, such as LIM domain protein, can maintain the functional structure of cardiomyocytes by a mechanism involving its own binding and actin filament cross-linking, which plays an important role in the development of heart disease (Hoffmann et al, 2014)
The formation of protein complexes such as PDZ and LIM domain 5 (PDLIM5)/PKC/Protein kinase LIM D1 (PKD1) is well understood, the downstream molecular events remain to be elucidated. These results suggest that the localization of PDLIM5 at some subcellular sites and its ability to interact with multiple functional proteins play an important role in cellular and physiological functions
Summary
PDZ and LIM domain 5 ( known as ENH, ENH1, L9, and LIM) is a cytoskeleton-related protein that was first discovered by Kuroda et al (1996), using yeast two-hybrid technology with protein kinase C (PKC) as the bait protein. Mouse PDLIM5 isoform I (mENH-1) encodes a full-length 591-amino-acid protein containing a PDZ domain and three LIM domains; two smaller transcripts, called mouse PDLIM5 isoform 2 and 3 (mENH-2 and mENH-3), encode a 337amino-acid protein and a 239-amino-acid protein, respectively. Both mouse PDLIM5 isoforms 2 and 3 lack three LIM domains (Niederlander et al, 2004; Zheng et al, 2010). The PDLIM5 protein, known as ENH, is a member of the Enigma family, which consists of an N-terminal PDZ domain and three C-terminal LIM domains. The PDZ domain, one of the most common protein-protein binding domains, is characterized by a highly conserved 80-90 amino acid sequence, consisting of six anti-parallel β-strands and two α-helices
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