TY - JOUR
T1 - The Arf GTPase-activating protein SMAP1 promotes transferrin receptor endocytosis and interacts with SMAP2
AU - Kobayashi, Nobuhide
AU - Kon, Shunsuke
AU - Henmi, Yuji
AU - Funaki, Tomo
AU - Satake, Masanobu
AU - Tanabe, Kenji
N1 - Funding Information:
This work was supported by research Grants from the Ministry of Education, Science, Sports, Culture and Technology of Japan ; Astellas Foundation for Research on Metabolic Disorders ; and Takeda Science Foundation , Japan.
Publisher Copyright:
© 2014 Elsevier Inc. All rights reserved.
PY - 2014/10/24
Y1 - 2014/10/24
N2 - Arf GTPase-activating proteins (Arf GAP) play important roles in the formation of the membrane vesicles that traffic between subcellular membranous organelles. The small Arf GTPase-activating protein (SMAP) subfamily of Arf GAPs has two members, SMAP1 and SMAP2, in mammals. The present study investigated whether these two proteins may have an overlapping function in addition to their previously reported distinct functions. Results showed that the presence of either SMAP1 or SMAP2 was sufficient for endocytosis of the transferrin receptor, and that transferrin incorporation was impaired only by the absence of both SMAP1 and SMAP2. This suggests the involvement of both SMAP1 and SMAP2 in transferrin endocytosis. Results also demonstrated a physical association between SMAP1 and SMAP2, which might serve as a basis for a functional interaction, and identified the intramolecular domains responsible for this association.
AB - Arf GTPase-activating proteins (Arf GAP) play important roles in the formation of the membrane vesicles that traffic between subcellular membranous organelles. The small Arf GTPase-activating protein (SMAP) subfamily of Arf GAPs has two members, SMAP1 and SMAP2, in mammals. The present study investigated whether these two proteins may have an overlapping function in addition to their previously reported distinct functions. Results showed that the presence of either SMAP1 or SMAP2 was sufficient for endocytosis of the transferrin receptor, and that transferrin incorporation was impaired only by the absence of both SMAP1 and SMAP2. This suggests the involvement of both SMAP1 and SMAP2 in transferrin endocytosis. Results also demonstrated a physical association between SMAP1 and SMAP2, which might serve as a basis for a functional interaction, and identified the intramolecular domains responsible for this association.
KW - Arf GTPase-activating protein
KW - Clathrin
KW - Endocytosis
KW - Membrane traffic
KW - Transferrin receptor
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U2 - 10.1016/j.bbrc.2014.09.108
DO - 10.1016/j.bbrc.2014.09.108
M3 - Article
C2 - 25281535
AN - SCOPUS:84918524030
VL - 453
SP - 473
EP - 479
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -