PMID- 18719403
OWN - NLM
STAT- MEDLINE
DCOM- 20101130
LR  - 20211020
IS  - 1933-6942 (Electronic)
IS  - 1933-6934 (Print)
IS  - 1933-6934 (Linking)
VI  - 2
IP  - 4
DP  - 2008 Jul-Aug
TI  - The Drosophila protein palmitoylome: characterizing palmitoyl-thioesterases and 
      DHHC palmitoyl-transferases.
PG  - 198-214
AB  - Palmitoylation is the post-translational addition of a palmitate moiety to a 
      cysteine residue through a covalent thioester bond. The addition and removal of 
      this modification is controlled by both palmitoyl acyl-transferases and 
      thioesterases. Using bioinformatic analysis, we identified 22 DHHC family 
      palmitoyl acyl-transferase homologs in the Drosophila genome. We used in situ 
      hybridization,RT-PCR, and published FlyAtlas microarray data to characterize the 
      expression patterns of all 22 fly homologs. Our results indicate that all are 
      expressed genes, but several, including CG1407, CG4676, CG5620, CG6017/dHIP14, 
      CG6618, CG6627 and CG17257 appear to be enriched in neural tissues suggesting 
      that they are important for neural function. Furthermore, we have found that 
      several may be expressed in a sex-specific manner with adult male specific 
      expression of CG4483 and CG17195. Using tagged versions of the DHHC genes, we 
      demonstrate that fly DHHC proteins are primarily located in either the Golgi 
      Apparatus or Endoplasmic Reticulum in S2 cells, except for CG1407, which was 
      found on the plasma membrane. We also characterized the subcellular localization 
      and expression of the three known thioesterases: Palmitoyl-protein Thioesterase 1 
      (Ppt1), Palmitoyl-protein Thioesterase 2 (Ppt2)and Acyl-protein Thioesterase 1 
      (APT1). Our results indicate that Ppt1 and Ppt2 are the major lysosomal 
      thioesterases while APT1 is the likely cytoplasmic thioesterase. Finally, in vivo 
      rescue experiments show that Ppt2 expression cannot rescue the neural inclusion 
      phenotypes associated with loss of Ppt1, further supporting distinct functions 
      and substrates for these two thioesterases. These results will serve as the basis 
      for a more complete understanding of the protein palmitoylome's normal cellular 
      functions in the fly and will lead to further insights into the molecular 
      etiology of diseases associated with the mis-regulation of palmitoylation.
FAU - Bannan, Barbra A
AU  - Bannan BA
AD  - Department of Biology; College of Charleston; Charleston, South Carolina, USA.
FAU - Van Etten, Jamie
AU  - Van Etten J
FAU - Kohler, John A
AU  - Kohler JA
FAU - Tsoi, Yui
AU  - Tsoi Y
FAU - Hansen, Nicole M
AU  - Hansen NM
FAU - Sigmon, Stacey
AU  - Sigmon S
FAU - Fowler, Elizabeth
AU  - Fowler E
FAU - Buff, Haley
AU  - Buff H
FAU - Williams, Tiffany S
AU  - Williams TS
FAU - Ault, Jeffrey G
AU  - Ault JG
FAU - Glaser, Robert L
AU  - Glaser RL
FAU - Korey, Christopher A
AU  - Korey CA
LA  - eng
GR  - R21 NS044572/NS/NINDS NIH HHS/United States
GR  - NS44572/NS/NINDS NIH HHS/United States
GR  - R15-HD052362/HD/NICHD NIH HHS/United States
GR  - R15 HD052362-01/HD/NICHD NIH HHS/United States
GR  - P20-RR16461/RR/NCRR NIH HHS/United States
GR  - P20 RR016461/RR/NCRR NIH HHS/United States
GR  - R15 HD052362/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - United States
TA  - Fly (Austin)
JT  - Fly
JID - 101470897
RN  - 0 (Drosophila Proteins)
RN  - 0 (Membrane Proteins)
RN  - EC 2.3.- (Acyltransferases)
RN  - EC 3.1.2.- (Thiolester Hydrolases)
RN  - EC 3.1.2.2 (Palmitoyl-CoA Hydrolase)
RN  - EC 3.1.2.22 (Ppt1 protein, Drosophila)
RN  - EC 3.1.2.22 (palmitoyl-protein thioesterase)
SB  - IM
MH  - Acyltransferases/genetics/*metabolism
MH  - Amino Acid Motifs
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cell Line
MH  - Drosophila/*enzymology/genetics/growth & development
MH  - Drosophila Proteins/genetics/*metabolism
MH  - Genes, Insect
MH  - Humans
MH  - Male
MH  - Membrane Proteins/genetics/*metabolism
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - Palmitoyl-CoA Hydrolase/genetics/*metabolism
MH  - Thiolester Hydrolases/genetics/*metabolism
PMC - PMC2898910
MID - NIHMS186487
EDAT- 2008/08/23 09:00
MHDA- 2010/12/14 06:00
PMCR- 2010/07/07
CRDT- 2008/08/23 09:00
PHST- 2008/08/23 09:00 [pubmed]
PHST- 2010/12/14 06:00 [medline]
PHST- 2008/08/23 09:00 [entrez]
PHST- 2010/07/07 00:00 [pmc-release]
AID - 6621 [pii]
AID - 10.4161/fly.6621 [doi]
PST - ppublish
SO  - Fly (Austin). 2008 Jul-Aug;2(4):198-214. doi: 10.4161/fly.6621.