The Experts below are selected from a list of 312 Experts worldwide ranked by ideXlab platform
Tatsuji Nishihara - One of the best experts on this subject based on the ideXlab platform.
-
lysophosphatidylethanolamine acyltransferase 1 membrane bound o acyltransferase 1 regulates morphology and function of p19c6 cell derived neurons
The FASEB Journal, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Tomomi Hashidateyoshida, Hideo Shindou, Toshinori Okinaga, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)–treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 c...
-
Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell–derived neurons
The FASEB Journal, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Hideo Shindou, Toshinori Okinaga, Tomomi Hashidate-yoshida, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)–treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 c...
-
Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell–derived neurons
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Hideo Shindou, Toshinori Okinaga, Tomomi Hashidate-yoshida, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)-treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 cells. Voltage-dependent calcium channel activity was also suppressed in these cells transfected with LPEAT1/MBOAT1 siRNA. These results suggest that LPEAT1/MBOAT1 plays an important role in neurite outgrowth and function.-Tabe, S., Hikiji, H., Ariyoshi, W., Hashidate-Yoshida, T., Shindou, H., Okinaga, T., Shimizu, T., Tominaga, K., Nishihara, T. Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell-derived neurons.
Shirou Tabe - One of the best experts on this subject based on the ideXlab platform.
-
lysophosphatidylethanolamine acyltransferase 1 membrane bound o acyltransferase 1 regulates morphology and function of p19c6 cell derived neurons
The FASEB Journal, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Tomomi Hashidateyoshida, Hideo Shindou, Toshinori Okinaga, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)–treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 c...
-
Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell–derived neurons
The FASEB Journal, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Hideo Shindou, Toshinori Okinaga, Tomomi Hashidate-yoshida, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)–treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 c...
-
Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell–derived neurons
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Hideo Shindou, Toshinori Okinaga, Tomomi Hashidate-yoshida, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)-treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 cells. Voltage-dependent calcium channel activity was also suppressed in these cells transfected with LPEAT1/MBOAT1 siRNA. These results suggest that LPEAT1/MBOAT1 plays an important role in neurite outgrowth and function.-Tabe, S., Hikiji, H., Ariyoshi, W., Hashidate-Yoshida, T., Shindou, H., Okinaga, T., Shimizu, T., Tominaga, K., Nishihara, T. Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell-derived neurons.
Wataru Ariyoshi - One of the best experts on this subject based on the ideXlab platform.
-
lysophosphatidylethanolamine acyltransferase 1 membrane bound o acyltransferase 1 regulates morphology and function of p19c6 cell derived neurons
The FASEB Journal, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Tomomi Hashidateyoshida, Hideo Shindou, Toshinori Okinaga, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)–treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 c...
-
Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell–derived neurons
The FASEB Journal, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Hideo Shindou, Toshinori Okinaga, Tomomi Hashidate-yoshida, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)–treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 c...
-
Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell–derived neurons
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Hideo Shindou, Toshinori Okinaga, Tomomi Hashidate-yoshida, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)-treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 cells. Voltage-dependent calcium channel activity was also suppressed in these cells transfected with LPEAT1/MBOAT1 siRNA. These results suggest that LPEAT1/MBOAT1 plays an important role in neurite outgrowth and function.-Tabe, S., Hikiji, H., Ariyoshi, W., Hashidate-Yoshida, T., Shindou, H., Okinaga, T., Shimizu, T., Tominaga, K., Nishihara, T. Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell-derived neurons.
Takao Shimizu - One of the best experts on this subject based on the ideXlab platform.
-
lysophosphatidylethanolamine acyltransferase 1 membrane bound o acyltransferase 1 regulates morphology and function of p19c6 cell derived neurons
The FASEB Journal, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Tomomi Hashidateyoshida, Hideo Shindou, Toshinori Okinaga, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)–treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 c...
-
Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell–derived neurons
The FASEB Journal, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Hideo Shindou, Toshinori Okinaga, Tomomi Hashidate-yoshida, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)–treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 c...
-
Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell–derived neurons
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Hideo Shindou, Toshinori Okinaga, Tomomi Hashidate-yoshida, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)-treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 cells. Voltage-dependent calcium channel activity was also suppressed in these cells transfected with LPEAT1/MBOAT1 siRNA. These results suggest that LPEAT1/MBOAT1 plays an important role in neurite outgrowth and function.-Tabe, S., Hikiji, H., Ariyoshi, W., Hashidate-Yoshida, T., Shindou, H., Okinaga, T., Shimizu, T., Tominaga, K., Nishihara, T. Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell-derived neurons.
Kazuhiro Tominaga - One of the best experts on this subject based on the ideXlab platform.
-
lysophosphatidylethanolamine acyltransferase 1 membrane bound o acyltransferase 1 regulates morphology and function of p19c6 cell derived neurons
The FASEB Journal, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Tomomi Hashidateyoshida, Hideo Shindou, Toshinori Okinaga, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)–treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 c...
-
Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell–derived neurons
The FASEB Journal, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Hideo Shindou, Toshinori Okinaga, Tomomi Hashidate-yoshida, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)–treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 c...
-
Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell–derived neurons
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2016Co-Authors: Shirou Tabe, Hisako Hikiji, Wataru Ariyoshi, Hideo Shindou, Toshinori Okinaga, Tomomi Hashidate-yoshida, Kazuhiro Tominaga, Takao Shimizu, Tatsuji NishiharaAbstract:Glycerophospholipids, which are components of Biomembranes, are formed de novo by the Kennedy pathway and subsequently mature through the Lands cycle. Lysophospholipid acyltransferases (LPLATs) are key enzymes in both pathways and influence the fatty acid composition of Biomembranes. Neuronal differentiation is characterized by neurite outgrowth, which requires Biomembrane biosynthesis. However, the role of LPLATs in neuronal differentiation remains unknown. In this study, we examined whether LPLATs are involved in neuronal differentiation using all-trans-retinoic acid (ATRA)-treated P19C6 cells. In these cells, mRNA levels of lysophosphatidylethanolamine acyltransferase (LPEAT)-1/membrane-bound O-acyltransferase (MBOAT)-1 were higher than those in undifferentiated cells. LPEAT enzymatic activity increased with 16:0- and 18:1-CoA as acyl donors. When LPEAT1/MBOAT1 was knocked down with small interfering RNA (siRNA), outgrowth of neurites and expression of neuronal markers decreased in ATRA-treated P19C6 cells. Voltage-dependent calcium channel activity was also suppressed in these cells transfected with LPEAT1/MBOAT1 siRNA. These results suggest that LPEAT1/MBOAT1 plays an important role in neurite outgrowth and function.-Tabe, S., Hikiji, H., Ariyoshi, W., Hashidate-Yoshida, T., Shindou, H., Okinaga, T., Shimizu, T., Tominaga, K., Nishihara, T. Lysophosphatidylethanolamine acyltransferase 1/membrane-bound O-acyltransferase 1 regulates morphology and function of P19C6 cell-derived neurons.