Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis
- J. Vesa, E. Hellsten, L. Peltonen
- Biology, MedicineNature
- 17 August 1995
The identification, by positional candidate methods, of defects in the palmitoyl-protein thioesterase gene in all 42 Finnish INCL patients and several non-Finnish patients is reported, which results in intracellular accumulation of the polypeptide and undetectable enzyme activity in the brain of patients.
Disruption of PPT1 or PPT2 causes neuronal ceroid lipofuscinosis in knockout mice
- Praveena K. Gupta, A. Soyombo, S. Hofmann
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 20 November 2001
These studies provide a mouse model for infantile neuronal ceroid lipofuscinosis and further suggest that PPT2 serves a role in the brain that is not carried out by PPT1.
Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras.
- L. A. Camp, S. Hofmann
- BiologyJournal of Biological Chemistry
- 25 October 1993
DHHC5 Protein Palmitoylates Flotillin-2 and Is Rapidly Degraded on Induction of Neuronal Differentiation in Cultured Cells*
- Yi Li, Brent R. Martin, B. Cravatt, S. Hofmann
- BiologyJournal of Biological Chemistry
- 11 November 2011
It is found that down-regulation of DHHC5 was triggered within minutes following growth factor withdrawal from normal neural stem cells, a maneuver that is used to induce neural differentiation in culture and suggest that protein palmitoylation can be regulated through changes in DHHC PAT levels in response to differentiation signals.
Progressively reduced synaptic vesicle pool size in cultured neurons derived from neuronal ceroid lipofuscinosis-1 knockout mice
- T. Virmani, Praveena K. Gupta, Xinran Liu, E. Kavalali, S. Hofmann
- BiologyNeurobiology of Disease
- 1 November 2005
Molecular cloning and expression of palmitoyl-protein thioesterase.
- L. A. Camp, L. Verkruyse, S. Afendis, C. Slaughter, S. Hofmann
- BiologyJournal of Biological Chemistry
- 16 September 1994
While thePalmitoyl-protein thioesterase will deacylate intracellular palmitoylated proteins such as Ha-Ras and the alpha subunits of heterotrimeric G proteins, the physiologic substrates are likely to be externally oriented or secreted proteins.
Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S.
- A. Das, C. Becerra, S. Hofmann
- Biology, MedicineJournal of Clinical Investigation
- 15 July 1998
In 29 of the families, PPT deficiency was found to be responsible for the neurodegenerative disorder, and mutations were identified in 57 out of 58 PPT alleles, resulting in a broader spectrum of clinical presentations than previously seen in the Finnish population.
DHHC5 Interacts with PDZ Domain 3 of Post-synaptic Density-95 (PSD-95) Protein and Plays a Role in Learning and Memory*
- Yi Li, Jie Hu, S. Hofmann
- BiologyJournal of Biological Chemistry
- 22 February 2010
It is reported that mice homozygous for a hypomorphic allele of a previously uncharacterized member, DHHC5, are born at half the expected rate, and survivors show a marked deficit in contextual fear conditioning, an indicator of defective hippocampal-dependent learning.
The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis.
- J. Bellizzi, J. Widom, J. Clardy
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 25 April 2000
The crystal structure of PPT1 with and without bound palmitate is determined by using multiwavelength anomalous diffraction phasing and reveals an alpha/beta-hydrolase fold with a catalytic triad composed of Ser115-His289-Asp233 and provides insights into the structural basis for the phenotypes associated with P PT1 mutations.
Massive palmitoylation-dependent endocytosis during reoxygenation of anoxic cardiac muscle
- Mei-Jung Lin, Michael Fine, Jui-Yun Lu, S. Hofmann, G. Frazier, D. Hilgemann
- BiologyeLife
- 26 November 2013
The MEND pathway appears to be deleterious in severe oxidative stress but may constitutively contribute to cardiac sarcolemma turnover in dependence on metabolic stress.
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