ER‐resident G<sub>i2</sub> protein controls sar1 translocation onto the ER during budding of transport vesicles

Nakagawa, Hiroshi; Umadome, Haruka; Miyazaki, Shunichi; Tanaka, Katsuhiro; Nishimura, Kazuhiko; Komori, Masaharu; Matsuo, Saburo

doi:10.1002/jcb.23142

Cited by 4 publications

(1 citation statement)

References 48 publications

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“…However, the involvement of Gβγ in UPR in mammalian cells has yet to be demonstrated. Lastly, a recent report linked Gα i2 to the small GTPase Sar1, a protein that regulates the generation of COPII vesicles from the ER membrane which are destined to the Golgi [95]. It was shown that the Gi protein activator, mastoparan 7, suppressed the translocation of Sar1 to the ER in a cell free, microsomal system, while a negative regulator of the Gi protein, pertussis toxin, recovered this suppression.…”

Section: G Proteins At Organellesmentioning

confidence: 99%

Non-canonical signaling and localizations of heterotrimeric G proteins

Hewavitharana¹,

Wedegaertner²

2012

Cellular Signalling

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Heterotrimeric G proteins typically transduce signals from G protein-coupled receptors (GPCRs) to effector proteins. In the conventional G protein signaling paradigm, the G protein is located at the cytoplasmic surface of the plasma membrane, where, after activation by an agonist-bound GPCR, the GTP-bound Gα and free Gβγ bind to and regulate a number of well-studied effectors, including adenylyl cyclase, phospholipase Cβ, RhoGEFs and ion channels. However, research over the past decade or more has established that G proteins serve non-canonical roles in the cell, whereby they regulate novel effectors, undergo activation independently of a GPCR, and/or function at subcellular locations other than the plasma membrane. This review will highlight some of these non-canonical aspects of G protein signaling, focusing on direct interactions of G protein subunits with cytoskeletal and cell adhesion proteins, the role of G proteins in cell division, and G protein signaling at diverse organelles.

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Section: G Proteins At Organellesmentioning

confidence: 99%

Non-canonical signaling and localizations of heterotrimeric G proteins

Hewavitharana¹,

Wedegaertner²

2012

Cellular Signalling

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On the segregation of protein ionic residues by charge type

2012

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Based on ubiquitous presence of large ionic motifs and clusters in proteins involved in gene transcription and protein synthesis, we analyzed the distribution of ionizable sidechains in a broad selection of proteins with regulatory, metabolic, structural and adhesive functions, in agonist, antagonist, toxin and antimicrobial peptides, and in self-excising inteins and intron-derived proteins and sequence constructs. All tested groups, regardless of taxa or sequence size, show considerable segregation of ionizable sidechains into same type charge (homoionic) tracts. These segments in most cases exceed half of the sequence length and comprise more than two-thirds of all ionizable sidechains. This distribution of ionic residues apparently reflects a fundamental advantage of sorted electrostatic contacts in association of sequence elements within and between polypeptides, as well as in interaction with polynucleotides. While large ionic densities are encountered in highly interactive proteins, the average ionic density in most sets does not change appreciably with size of the homoionic segments, which supports the segregation as a modular feature favoring association.

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Sar1 translocation onto the ER-membrane for vesicle budding has different pathways for promotion and suppression of ER-to-Golgi transport mediated through H89-sensitive kinase and ER-resident G protein

et al. 2012

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ER-to-Golgi protein transport involves transport vesicles of which formation is initiated by assembly of Sar1. The assembly of Sar1 is suppressed by protein kinase inhibitor H89, suggesting that ER-to-Golgi transport is regulated progressively by H89 sensitive kinase. ER-resident G(i2) protein suppresses vesicle formation with inhibition of Sar1 assembly. This study examined whether these promotion and suppression of vesicle transport share the same signal pathway, by examining the effects of G(i/o) protein activator mastoparan 7 (Mp-7) and H89 on Sar1 and Sec23 recruitment onto microsomes. In a cell-free system for Sar1 translocation assay, GTPγS addition induced the translocation of Sar1 onto microsomes. Mp-7 and H89 decreased the Sar1 translocation. Double treatment of Mp-7 and H89 strongly decreased Sar1 translocation. In single and double treatments, however, G(i/o) protein inactivator pertussis toxin (IAP) partially restored the suppressive effect of Mp-7, but had not any effect on H89-induced effect. Then, the assembly of Sec23 onto the microsome was also increased by the addition of GTPγS. Sec23 translocation was decreased by Mp-7 and/or H89 treatment and recovered by IAP pretreatment except for H89 single treatment, similarly to Sar1 translocation in each treatment. Inhibitory effects of H89 and Mp-7on ER-to-Golgi vesicle transport by H89 or Mp-7 were also confirmed in a cell culture system by BFA-dispersion and BFA-reconstruction experiments. These findings indicate that promotion and suppression of ER-to-Golgi vesicle transport are modulated through separate signal pathways.

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ER‐resident G_i2 protein controls sar1 translocation onto the ER during budding of transport vesicles

Cited by 4 publications

References 48 publications

Non-canonical signaling and localizations of heterotrimeric G proteins

Non-canonical signaling and localizations of heterotrimeric G proteins

On the segregation of protein ionic residues by charge type

Sar1 translocation onto the ER-membrane for vesicle budding has different pathways for promotion and suppression of ER-to-Golgi transport mediated through H89-sensitive kinase and ER-resident G protein

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ER‐resident Gi2 protein controls sar1 translocation onto the ER during budding of transport vesicles

Cited by 4 publications

References 48 publications

Non-canonical signaling and localizations of heterotrimeric G proteins

Non-canonical signaling and localizations of heterotrimeric G proteins

On the segregation of protein ionic residues by charge type

Sar1 translocation onto the ER-membrane for vesicle budding has different pathways for promotion and suppression of ER-to-Golgi transport mediated through H89-sensitive kinase and ER-resident G protein

Contact Info

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ER‐resident G_i2 protein controls sar1 translocation onto the ER during budding of transport vesicles