TY - JOUR
T1 - The dynamic structure of Rab35 is stabilized in the presence of GTP under physiological conditions
AU - Murata, Takuya
AU - Unno, Yuka
AU - Fukuda, Mitsunori
AU - Utsunomiya-Tate, Naoko
N1 - Funding Information:
This work was supported by research activity of Teikyo University .
Publisher Copyright:
© 2020 The Authors
PY - 2020/9
Y1 - 2020/9
N2 - Rab proteins, a family of small guanosine triphosphatases, play key roles in intracellular membrane trafficking and the regulation of various cellular processes. As a Rab isoform, Rab35 is crucial for recycling endosome trafficking, cytokinesis and neurite outgrowth. In this report, we analyzed dynamic structural changes and physicochemical features of Rab35 in response to different external conditions, including temperature, pH, salt concentration and guanosine triphosphate (GTP), by circular dichroism (CD) spectroscopy. CD spectra revealed that the α-helix content of Rab35 varies under different conditions considerably. The addition of GTP increases the α-helix content of Rab35 when the temperature, pH and salt concentration match physiological conditions. The results suggest that the external environment affects the secondary structure of Rab35. In particular, the presence of GTP stabilized the α-helices of Rab35 under physiological conditions. These structural changes may translate to changes in Rab35 function and relate to its role in membrane trafficking.
AB - Rab proteins, a family of small guanosine triphosphatases, play key roles in intracellular membrane trafficking and the regulation of various cellular processes. As a Rab isoform, Rab35 is crucial for recycling endosome trafficking, cytokinesis and neurite outgrowth. In this report, we analyzed dynamic structural changes and physicochemical features of Rab35 in response to different external conditions, including temperature, pH, salt concentration and guanosine triphosphate (GTP), by circular dichroism (CD) spectroscopy. CD spectra revealed that the α-helix content of Rab35 varies under different conditions considerably. The addition of GTP increases the α-helix content of Rab35 when the temperature, pH and salt concentration match physiological conditions. The results suggest that the external environment affects the secondary structure of Rab35. In particular, the presence of GTP stabilized the α-helices of Rab35 under physiological conditions. These structural changes may translate to changes in Rab35 function and relate to its role in membrane trafficking.
KW - Circular dichroism spectroscopy
KW - Guanosine triphosphate
KW - Rab35
KW - Secondary structure
KW - α-Helix
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U2 - 10.1016/j.bbrep.2020.100776
DO - 10.1016/j.bbrep.2020.100776
M3 - Article
AN - SCOPUS:85087072189
SN - 2405-5808
VL - 23
JO - Biochemistry and Biophysics Reports
JF - Biochemistry and Biophysics Reports
M1 - 100776
ER -