Phosphorylation of the Bin, Amphiphysin, and RSV161/167 (BAR) domain of ACAP4 regulates membrane tubulation

Zhao, Xuannv; Wang, Dongmei; Liu, Xing; Liu, Lifang; Song, Zhenwei; Zhu, Tongge; Adams, Gregory; Gao, Xiaolan; Tian, Ruijun; Huang, Yunpeng; Chen, Runhua; Wang, Fengsong; Liu, Dong; Xue, Yu; Chen, Yong; Chen, Zhengjun; Teng, Maikun; Ding, Xia; Yao, Xuebiao

doi:10.1073/pnas.1217727110

Cited by 19 publications

(22 citation statements)

References 38 publications

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“…S3A; lanes 2-3 vs. 1). It has been reported that stimulation with epidermal growth factor (EGF) promotes membrane association of the BAR domain (35). We confirmed EGFR expression in our HEK293T cells, and EGFR level is down-regulated upon EGF stimulation as previously reported by Hong et al (36) (Supplemental Fig.…”

Section: Ptena Interacts With Endocytic Proteins and Regulates Endocysupporting

confidence: 91%

PTENα regulates endocytosis and modulates olfactory function

et al. 2019

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Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) α is the first identified isoform of the well‐known tumor suppressor PTEN. PTENα has an evolutionarily conserved 173‐aa N terminus compared with canonical PTEN. Recently, PTENα has been shown to play roles in multiple biologic processes including learning and memory, cardiac homeostasis, and antiviral immunity. Here, we report that PTENα maintains mitral cells in olfactory bulb (OB), regulates endocytosis in OB neurons, and controls olfactory behaviors in mice. We show that PTENα directly dephosphorylates the endocytic protein amphiphysin and promotes its binding to adaptor‐related protein complex 2 subunit β1 (Ap2b1). In addition, we identified mutations in the N terminus of PTENα in patients with Parkinson disease and Lewy‐body dementia, which are neurodegenerative disorders with early olfactory loss. Overexpression of PTENα mutant H169N in mice OB reduces odor sensitivity. Our data demonstrate a role of PTENα in olfactory function and provide insight into the mechanism of olfactory dysfunction in neurologic disorders.—Yuan, Y., Zhao, X., Wang, P., Mei, F., Zhou, J., Jin, Y., McNutt, M. A., Yin, Y. PTENα regulates endocytosis and modulates olfactory function. FASEB J. 33, 11148–11162 (2019). http://www.fasebj.org

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Section: Ptena Interacts With Endocytic Proteins and Regulates Endocysupporting

confidence: 91%

PTENα regulates endocytosis and modulates olfactory function

et al. 2019

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“…A large number of cytosolic proteins are known to be activated and transduce signals upon phosphorylation or the addition of a charge to the protein. Recently, the BAR domains of ACAP4 have been reported to be activated by phosphorylation during membrane association in a manner dependent on epidermal growth factor (EGF) stimulation (333). However, when we consider the increase of negative charge brought by phosphorylation, the consequence might be the opposite, because an addition of negative charge may enhance repulsion from anionic lipids of the membrane.…”

Section: F How Is the Bar Domain Superfamily Regulated?mentioning

confidence: 99%

Dynamic Shaping of Cellular Membranes by Phospholipids and Membrane-Deforming Proteins

Suetsugu

Kurisu

Takenawa

2014

Physiological Reviews

206

207

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All cellular compartments are separated from the external environment by a membrane, which consists of a lipid bilayer. Subcellular structures, including clathrin-coated pits, caveolae, filopodia, lamellipodia, podosomes, and other intracellular membrane systems, are molded into their specific submicron-scale shapes through various mechanisms. Cells construct their micro-structures on plasma membrane and execute vital functions for life, such as cell migration, cell division, endocytosis, exocytosis, and cytoskeletal regulation. The plasma membrane, rich in anionic phospholipids, utilizes the electrostatic nature of the lipids, specifically the phosphoinositides, to form interactions with cytosolic proteins. These cytosolic proteins have three modes of interaction: 1) electrostatic interaction through unstructured polycationic regions, 2) through structured phosphoinositide-specific binding domains, and 3) through structured domains that bind the membrane without specificity for particular phospholipid. Among the structured domains, there are several that have membrane-deforming activity, which is essential for the formation of concave or convex membrane curvature. These domains include the amphipathic helix, which deforms the membrane by hemi-insertion of the helix with both hydrophobic and electrostatic interactions, and/or the BAR domain superfamily, known to use their positively charged, curved structural surface to deform membranes. Below the membrane, actin filaments support the micro-structures through interactions with several BAR proteins as well as other scaffold proteins, resulting in outward and inward membrane micro-structure formation. Here, we describe the characteristics of phospholipids, and the mechanisms utilized by phosphoinositides to regulate cellular events. We then summarize the precise mechanisms underlying the construction of membrane micro-structures and their involvements in physiological and pathological processes.

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“…Dry glue was prepared through Coomassie blue staining, and the phosphor screen was pressed. A typhoon scanner was used for data analysis (Ren and Dai , Zhang et al , Zhao et al )…”

Section: Methodsmentioning

confidence: 99%

Functional study of a salt‐inducible TaSR gene in Triticum aestivum

Xiang

Cui

Zhao

et al. 2015

Physiologia Plantarum

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The gene expression chip of a salt-tolerant wheat mutant under salt stress was used to clone a salt-induced gene with unknown functions. This gene was designated as TaSR (Triticum aestivum salt-response gene) and submitted to GenBank under accession number EF580107. Quantitative polymerase chain reaction (PCR) analysis showed that gene expression was induced by salt stress. Arabidopsis and rice (Oryza sativa) plants expressing TaSR presented higher salt tolerance than the controls, whereas AtSR mutant and RNA interference rice plants were more sensitive to salt. Under salt stress, TaSR reduced Na(+) concentration and improved cellular K(+) and Ca(2+) concentrations; this gene was also localized on the cell membrane. β-Glucuronidase (GUS) staining and GUS fluorescence quantitative determination were conducted through fragmentation cloning of the TaSR promoter. Salt stress-responsive elements were detected at 588-1074 bp upstream of the start codon. GUS quantitative tests of the full-length promoter in different tissues indicated that promoter activity was highest in the leaf under salt stress. Bimolecular fluorescence complementation and yeast two-hybrid screening further showed the correlation of TaSR with TaPRK and TaKPP. In vitro phosphorylation of TaSR and TaPRK2697 showed that TaPRK2697 did not phosphorylate TaSR. This study revealed that the novel TaSR may be used to improve plant tolerance to salt stress.

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Phosphorylation of the Bin, Amphiphysin, and RSV161/167 (BAR) domain of ACAP4 regulates membrane tubulation

Cited by 19 publications

References 38 publications

PTENα regulates endocytosis and modulates olfactory function

PTENα regulates endocytosis and modulates olfactory function

Dynamic Shaping of Cellular Membranes by Phospholipids and Membrane-Deforming Proteins

Functional study of a salt‐inducible TaSR gene in Triticum aestivum

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