Localization of EFA6A, an exchange factor for Arf6, in Z-lines and sarcoplasmic reticulum membranes in addition to myofilaments in I-domains of skeletal myofibers of peri-natal mice

• Published in: Acta histochemica Vol. 126; no. 5-7; p. 152187
• Main Authors: Chomphoo, Surang, Sakagami, Hiroyuki, Kondo, Hisatake, Hipkaeo, Wiphawi
• Format: Journal Article
• Language: English
• Published: Germany Elsevier GmbH 01.10.2024
• Subjects: Actinin - metabolism; ADP-Ribosylation Factor 6; ADP-Ribosylation Factors - metabolism; Animals; EFA6A; Guanine Nucleotide Exchange Factors - metabolism; I-domain SRs; Immunohistochemistry; Mice; Muscle Fibers, Skeletal - metabolism; Myofibrils - metabolism; Perinatal mice; Sarcoplasmic Reticulum - metabolism; Z-lines; Immunohistochemistry; Z-lines; Perinatal mice; I-domain SRs; EFA6A
• ISSN: 0065-1281; 1618-0372; 1618-0372
• DOI: 10.1016/j.acthis.2024.152187

Membrane trafficking and actin-remodeling are critical for well-maintained integrity of the cell organization and activity, and they require Arf6 (ADP ribosylation factor 6) activated by GEF (guanine nucleotide exchange factor) including EFA6 (exchange factor for Arf6). In the present immuno-electron microscopic study following previous immunohistochemical study by these authors (Chomphoo et al., 2020) of in situ skeletal myoblasts and myotubes of pre-and perinatal mice, the immunoreactivity for EFA6A was found to be localized at Z-bands and sarcoplasmic reticulum (SR) membranes in I-domains as well as I-domain myofilaments of skeletal myofibers of perinatal mice. Based on the previous finding that EFA6 anchored on the neuronal postsynaptic density via α-actinin which is known to be shared by muscular Z-bands, the present finding suggests that EFA6A is also anchored on Z-bands via α-actinin and involved in the membrane trafficking and actin-remodeling in skeletal myofibers. The localization of EFA6A-immunoreactivity in I-domain SR suggests a differential function in the membrane traffic between the I- and A-domain intracellular membranes in perinatal skeletal myofibers.