ArticleMolecular biology of the cell2011
Subcellular Golgi localization of stathmin family proteins is promoted by a specific set of DHHC palmitoyl transferases.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 33 citations in OpenAlex.
- Fat traffic control: S-acylation in axonal transport.Molecular pharmacology · 2025Review
- Microtubules, Membranes, and Movement: New Roles for Stathmin-2 in Axon Integrity.Journal of neuroscience research · 2024Review
- Deficiency of copper responsive gene stmn4 induces retinal developmental defects.Cell biology and toxicology · 2024Article
- The Stathmin-2 membrane-targeting domain is required for axon protection and regulated degradation by DLK signaling.The Journal of biological chemistry · 2023Article
- S-Palmitoylation of Synaptic Proteins in Neuronal Plasticity in Normal and Pathological Brains.Cells · 2023Review
- Stathmin-2 Mediates Glucagon Secretion From Pancreatic α-Cells.Frontiers in endocrinology · 2020Article
- Regulation of dendrite morphology and excitatory synapse formation by zDHHC15.Journal of cell science · 2019Article
- Role of Palmitoylation of Postsynaptic Proteins in Promoting Synaptic Plasticity.Frontiers in molecular neuroscience · 2019Review
- Disruption of the Zdhhc9 intellectual disability gene leads to behavioural abnormalities in a mouse model.Experimental neurology · 2018Article
- Insights Into ProteinFrontiers in molecular neuroscience · 2018Review
- Roles of palmitoylation in axon growth, degeneration and regeneration.Journal of neuroscience research · 2017Review
- A novel non genomic glucocorticoid signaling mediated by a membrane palmitoylated glucocorticoid receptor cross talks with GnRH in gonadotrope cells.Scientific reports · 2017Article
- Palmitoylation of Progressive Rod-Cone Degeneration (PRCD) Regulates Protein Stability and Localization.The Journal of biological chemistry · 2016Article
- ZDHHC3 Tyrosine Phosphorylation Regulates Neural Cell Adhesion Molecule Palmitoylation.Molecular and cellular biology · 2016Article
- Palmitoylation controls DLK localization, interactions and activity to ensure effective axonal injury signaling.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Reversible Cysteine Acylation Regulates the Activity of Human Palmitoyl-Protein Thioesterase 1 (PPT1).PloS one · 2016Article
- Identification of palmitoyltransferase and thioesterase enzymes that control the subcellular localization of axon survival factor nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2).The Journal of biological chemistry · 2014Article
- Palmitoylation of the immunity related GTPase, Irgm1: impact on membrane localization and ability to promote mitochondrial fission.PloS one · 2014Article
- Article
- Design and characterization of modular scaffolds for tubulin assembly.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein palmitoylation is a reversible lipid modification that plays critical roles in protein sorting and targeting to specific cellular compartments. The neuronal microtubule-regulatory phosphoproteins of the stathmin family (SCG10/stathmin 2, SCLIP/stathmin 3, and RB3/stathmin 4) are peripheral proteins that fulfill specific and complementary roles in the formation and maturation of the nervous system. All neuronal stathmins are localized at the Golgi complex and at vesicles along axons and dendrites. Their membrane anchoring results from palmitoylation of two close cysteine residues present within their homologous N-terminal targeting domains. By preventing palmitoylation with 2-bromopalmitate or disrupting the integrity of the Golgi with brefeldin A, we were able to show that palmitoylation of stathmins 2 and 3 likely occurs at the Golgi and is crucial for their specific subcellular localization and trafficking. In addition, this membrane binding is promoted by a specific set of palmitoyl transferases that localize with stathmins 2 and 3 at the Golgi, directly interact with them, and enhance their membrane association. The subcellular membrane-associated microtubule-regulatory activity of stathmins might then be fine-tuned by extracellular stimuli controlling their reversible palmitoylation, which can be viewed as a crucial regulatory process for specific and local functions of stathmins in neurons.
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