Journal Article10.1038/NRM2084
Palmitoylation: policing protein stability and traffic
1K
TL;DR: Recent studies that have provided insights into the mechanisms that mediate the functional consequences of palmitate are reviewed.
read more
Abstract: Palmitate modifies both peripheral and integral membrane proteins and its addition can be permanent or transient, which makes it unique among the lipid modifications of proteins. The presence of palmitate on a protein affects how the protein interacts with lipids and proteins in a membrane compartment, and the reversibility of palmitoylation allows different modes of trafficking between membrane compartments. Here, we review recent studies that have provided insights into the mechanisms that mediate the functional consequences of this versatile modification.
read more
Chat with Paper
AI Agents for this Paper
Find similar papers on Google Scholar, PubMed and Arxiv
Write a critical review of this paper
Analyze citations of this paper to find unaddressed research gaps
Citations
Cellular Interactions in the Tumor Microenvironment: The Role of Secretome
Bianca Rodrigues da Cunha,Célia Domingos,Ana Carolina Buzzo Stefanini,Tiago Henrique,Giovana Mussi Polachini,Pedro Castelo-Branco,Eloiza H. Tajara +6 more
TL;DR: This work has shown that tumor-stroma communication occurs directly between cells or via a variety of molecules secreted, such as growth factors, cytokines, chemokines and microRNAs, which is an important source of key regulators of the tumorigenic process.
Importin α Partitioning to the Plasma Membrane Regulates Intracellular Scaling
TL;DR: It is shown that the nuclear transport receptor importin α is modified by palmitoylation, which targets it to the plasma membrane and modulates its binding to nuclear localization signal (NLS)-containing proteins that regulate nuclear and spindle size in Xenopus egg extracts.
113
BAR domains, amphipathic helices and membrane‐anchored proteins use the same mechanism to sense membrane curvature
TL;DR: This work describes two different MCS protein motifs (amphipathic helices and BAR domains) and suggests that in both cases curvature sensitive membrane binding results from asymmetric insertion of hydrophobic amino acids in the lipid membrane.
108
Pathological implication of protein post-translational modifications in cancer.
Sheng Pan,Ru-Hong Chen +1 more
TL;DR: Protein post-translational modifications (PTMs) profoundly influence protein functions and play crucial roles in essentially all cell biological processes as discussed by the authors , and their crosstalk is linked to many critical signaling events involved in neoplastic transformation, carcinogenesis and metastasis.
108
Targeting Stimulator of Interferon Genes (STING): A Medicinal Chemistry Perspective
Han Zhang,Qidong You,Xiao-Li Xu +2 more
TL;DR: The current understanding of STING structure is summarized, the status quo of STings modulators is surveyed, established bioassay methods are compared, the chemical structures and bioactivities of agonists and inhibitors are reviewed, and suggestions and insights for the future exploitation of STing modulators are proposed.
105
References
The Ubiquitin System
Avram Hershko,Aaron Ciechanover +1 more
TL;DR: This review discusses recent information on functions and mechanisms of the ubiquitin system and focuses on what the authors know, and would like to know, about the mode of action of ubi...
Basic Medical Research Award. The ubiquitin system.
TL;DR: The ubiquitin system plays important roles in the control of numerous processes, including cell-cycle progression, signal transduction, transcriptional regulation, receptor down-regulation, and endocytosis as mentioned in this paper.
3.8K
Protein prenylation: molecular mechanisms and functional consequences.
Fang L. Zhang,Patrick J. Casey +1 more
TL;DR: The emphasis in this review is on the enzymology of prenyl protein processing and the functional significance ofPrenylation in cellular events.
2.1K
Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins.
TL;DR: The role of myristate and palmitate in promoting membrane binding as well as specific membrane targeting will be reviewed, with emphasis on the Src family of tyrosine protein kinases and alpha subunits of heterotrimeric G proteins.
1.3K
An Acylation Cycle Regulates Localization and Activity of Palmitoylated Ras Isoforms
Oliver Rocks,Anna Peyker,Martin Kahms,Peter J. Verveer,Carolin Koerner,Maria Lumbierres,Jürgen Kuhlmann,Herbert Waldmann,Alfred Wittinghofer,Philippe I. H. Bastiaens +9 more
TL;DR: It is shown that the specific subcellular distribution of H- and Nras guanosine triphosphate–binding proteins is generated by a constitutive de/reacylation cycle that operates on palmitoylated proteins, driving their rapid exchange between the plasma membrane (PM) and the Golgi apparatus.
881