3 results match your criteria palmitoylable residue

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AMPAR interacting protein CPT1C enhances surface expression of GluA1-containing receptors.

Front Cell Neurosci 2014 2;8:469. Epub 2015 Feb 2.

Laboratori de Neurobiologia, Area de Neurobiologia Cellular i Molecular, Institut d'Investigació Biomèdica de Bellvitge-IDIBELL L'Hospitalet de Llobregat, Spain ; Department of Pathology and Experimental Therapeutics, Faculty of Medicine, University of Barcelona L'Hospitalet de Llobregat, Spain.

AMPARs mediate the vast majority of fast excitatory synaptic transmission in the brain and their biophysical and trafficking properties depend on their subunit composition and on several posttranscriptional and posttranslational modifications. Additionally, in the brain AMPARs associate with auxiliary subunits, which modify the properties of the receptors. Despite the abundance of AMPAR partners, recent proteomic studies have revealed even more interacting proteins that could potentially be involved in AMPAR regulation. Read More

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February 2015

Interaction of the human prostacyclin receptor with Rab11: characterization of a novel Rab11 binding domain within alpha-helix 8 that is regulated by palmitoylation.

J Biol Chem 2010 Jun 15;285(24):18709-26. Epub 2010 Apr 15.

School of Biomolecular and Biomedical Sciences, Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland.

The human prostacyclin receptor (hIP) undergoes agonist-induced internalization and subsequent recyclization in slowly recycling endosomes involving its direct physical interaction with Rab11a. Moreover, interaction with Rab11a localizes to a 22-residue putative Rab11 binding domain (RBD) within the carboxyl-terminal tail of the hIP, proximal to the transmembrane 7 (TM7) domain. Because the proposed RBD contains Cys(308) and Cys(311), in addition to Cys(309), that are known to undergo palmitoylation, we sought to identify the structure/function determinants of the RBD, including the influence of palmitoylation, on agonist-induced trafficking of the hIP. Read More

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Distance-dependent cellular palmitoylation of de-novo-designed sequences and their translocation to plasma membrane subdomains.

J Cell Sci 2002 Aug;115(Pt 15):3119-30

Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense, 28040 Madrid, Spain.

Using recursive PCR, we created an artificial protein sequence that consists of a consensus myristoylation motif (MGCTLS) followed by the triplet AGS repeated nine times and fused to the GFP reporter. This linker-GFP sequence was utilized as a base to produce multiple mutants that were used to transfect COS-7 cells. Constructs where a 'palmitoylable' cysteine residue was progressively moved apart from the myristoylation site to positions 3, 9, 15 and 21 of the protein sequence were made, and these mutants were used to investigate the effect of protein myristoylation on subsequent palmitoylation, subcellular localization, membrane association and caveolin-1 colocalization. Read More

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