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Fig. 1 | Biomarker Research

Fig. 1

From: Pathophysiological roles of myristoylated alanine-rich C-kinase substrate (MARCKS) in hematological malignancies

Fig. 1

MARCKS protein structure. (a) The image was created from the protein data bank (PDB) entries 1IWQ [22] and adapted using PyMOL Version 2.2 [23]. (b) Linear representation of the MARCKS protein containing the Myristoyl Domain, N-terminal Domain, MH2 domain, a phosphorylation site domain (PSD; also known as the effector domain (ED)), and C-terminal Domain (c) Schematic representation of the MARCKS protein bound to the plasma membrane by the myristoylated N-terminal domain. Other structural elements include an MH2 domain and the ED. The ED (amino acids: 152–176) can be phosphorylated by PKC at three or four serine residues (marked in red) or can be bound to CaM and actin. The ED also electrostatically interacts with the plasma membrane and provides additional support to the N-terminal myristate moiety-mediated binding of MARCKS to the phospholipid bilayer of the membrane

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