TY - JOUR
T1 - Dynamic protein palmitoylation in cellular signaling
AU - Iwanaga, Tsuyoshi
AU - Tsutsumi, Ryouhei
AU - Noritake, Jun
AU - Fukata, Yuko
AU - Fukata, Masaki
N1 - Funding Information:
We thank Dr. David S. Bredt (Eli Lilly and Company) for the kind gift of PSD-95 cDNA, and Dr. Franck Perez (Curie Institut) for valuable discussion. R.T. and J.N. are supported by the Japan Society for the Promotion of Science. Y.F. is supported by grants from Human Frontier Science Program (HFSP CDA0015-07) and MEXT (18700376). M.F. is supported by grants from HFSP (RGY0059-06) and MEXT (20670005, 20022043, 20054022 and 18687008).
PY - 2009/5
Y1 - 2009/5
N2 - Protein S-palmitoylation, the most common lipid modification with the 16-carbon fatty acid palmitate, provides an important mechanism for regulating protein trafficking and function. The unique reversibility of protein palmitoylation allows proteins to rapidly shuttle between intracellular membrane compartments. Importantly, this palmitate cycling can be regulated by some physiological stimuli, contributing to cellular homeostasis and plasticity. Although the enzyme responsible for protein palmitoylation had been long elusive, DHHC family proteins, conserved from plants to mammals, have recently emerged as palmitoyl acyl transferases. Integrated approaches including advanced proteomics, live-cell imaging, and molecular genetics are beginning to clarify the molecular machinery for palmitoylation reaction in diverse aspects of cellular functions.
AB - Protein S-palmitoylation, the most common lipid modification with the 16-carbon fatty acid palmitate, provides an important mechanism for regulating protein trafficking and function. The unique reversibility of protein palmitoylation allows proteins to rapidly shuttle between intracellular membrane compartments. Importantly, this palmitate cycling can be regulated by some physiological stimuli, contributing to cellular homeostasis and plasticity. Although the enzyme responsible for protein palmitoylation had been long elusive, DHHC family proteins, conserved from plants to mammals, have recently emerged as palmitoyl acyl transferases. Integrated approaches including advanced proteomics, live-cell imaging, and molecular genetics are beginning to clarify the molecular machinery for palmitoylation reaction in diverse aspects of cellular functions.
KW - DHHC protein
KW - Lipid modification
KW - Palmitoyl acyl transferase
KW - Protein palmitoylation
KW - Protein targeting
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U2 - 10.1016/j.plipres.2009.02.001
DO - 10.1016/j.plipres.2009.02.001
M3 - Review article
C2 - 19233228
AN - SCOPUS:67349131266
VL - 48
SP - 117
EP - 127
JO - Progress in Lipid Research
JF - Progress in Lipid Research
SN - 0163-7827
IS - 3-4
ER -