Passive plasma membrane transporters play a critical role in perception of carbon availability in yeast

AbstractRecently, our lab found that the canonical glucose/galactose regulation pathway in yeast makes the decision to metabolize galactose based on the ratio of glucose to galactose concentrations in the external medium. This led to the question of where and how the ratio-sensing is achieved. Here, we consider the possibilities of an intracellular, extracellular, or membrane bound ratio sensing mechanisms. We show that hexose transporters in the plasma membrane are mainly responsible for glucose/galactose ratio-sensing in yeast. Further, while the glucose sensors Gpr1, Snf3, and Rgt2 are not required for ratio sensing, they help modulate the ratio sensing phenotype by regulating the expression of individual transporters in different environments. Our study provides an example of an unexpected, but potentially widespread, mechanism for making essential decisions.

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Regulation of Myosin-5b by Rab11a and the Rab11 family interacting protein 2

Bioscience Reports ◽

10.1042/bsr20181252 ◽

2019 ◽

Vol 39 (1) ◽

Cited By ~ 5

Author(s):

Huan-Hong Ji ◽

Lin-Lin Yao ◽

Chang Liu ◽

Xiang-dong Li

Keyword(s):

Plasma Membrane ◽

Motor Function ◽

Critical Role ◽

The Other ◽

Tail Domain ◽

Interacting Protein ◽

Other Hand ◽

Membrane Bound

Abstract Mammalian myosin-5b (Myo5b) plays a critical role in the recycling of endosomes to the plasma membrane via the interactions with Rab11a and the Rab11 family interacting protein 2 (FIP2). However, it remains unclear on how Rab11a and FIP2 are coordinated in tethering Myo5b with the vesicles and activating the motor function of Myo5b. In the present study, we show that Rab11a binds to the globular tail domain (GTD) of Myo5b and this binding abolishes the head–GTD interaction of Myo5b, thus activating the motor function of Myo5b. On the other hand, FIP2 directly interacts with both Rab11a and the tail of Myo5b, and the binding of FIP2 to Myo5b does not affect Myo5b motor function. Moreover, Rab11a displays higher affinity to FIP2 than to Myo5b, suggesting that Rab11a binds preferentially to FIP2 than to Myo5b. Based on the current findings, we propose that the association of Myo5b with vesicles is mediated by FIP2, which bridges Myo5b and the membrane-bound Rab11a, whereas the motor function of Myo5b is regulated by Rab11a.

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Plasma membrane bound transglutaminase in the marginal zone of psoriatic skin

Clinical and Experimental Dermatology ◽

10.1046/j.1365-2230.1999.00464.x ◽

1999 ◽

Vol 24 (3) ◽

pp. 237-239

Author(s):

Gerritsen ◽

Van Erp ◽

Van De Kerkhof

Keyword(s):

Plasma Membrane ◽

Marginal Zone ◽

Psoriatic Skin ◽

Membrane Bound

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Exterior and Interior Events in Early Stage of Thrombin-induced Platelet Aggregation

Thrombosis and Haemostasis ◽

10.1055/s-0038-1651878 ◽

1977 ◽

Vol 38 (03) ◽

pp. 0630-0639 ◽

Cited By ~ 4

Author(s):

Shuichi Hashimoto ◽

Sachiko Shibata ◽

Bonro Kobayashi

Keyword(s):

Molecular Weight ◽

Enzyme Activity ◽

Plasma Membrane ◽

Platelet Aggregation ◽

Early Stage ◽

Adenyl Cyclase ◽

Cellular Component ◽

Primary Event ◽

Rabbit Platelets ◽

Membrane Bound

SummaryTreatment of washed rabbit platelets with 1 u/ml of thrombin at 37° C resulted in a disappearance from platelets of a protein with 250,000 dalton molecular weight which was shown to be originated from plasma membrane. Parallel loss of adenyl cyclase was noted, and both reactions were complete within 30 sec. From the patterns of disc electrophoretograms, the importance of quick suppression of thrombin action in demonstrating the primary event was stressed.Thrombin induced an apparent activation of membrane bound phosphodiesterase. This reaction was also complete within 30 sec. The cellular component which contained the enzyme activity was distinct from plasma membrane. Soluble phosphodiesterase was not influenced by thrombin at all.These reactions required intact platelet cells to react with thrombin, and no reaction was detected when subcellular preparations were treated with thrombin.Possibility of collaboration of changes in externally located synthetic enzyme with those in internally located degrading enzyme in the early phase of thrombin action on platelets was suggested.

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RNF141 interacts with KRAS to promote colorectal cancer progression

Oncogene ◽

10.1038/s41388-021-01877-4 ◽

2021 ◽

Author(s):

Jiuna Zhang ◽

Xiaoyu Jiang ◽

Jie Yin ◽

Shiying Dou ◽

Xiaoli Xie ◽

...

Keyword(s):

Colorectal Cancer ◽

Plasma Membrane ◽

Tumor Growth ◽

Cancer Progression ◽

Critical Role ◽

Ring Finger ◽

Immunohistochemical Analysis ◽

Bimolecular Fluorescence Complementation

AbstractRING finger proteins (RNFs) play a critical role in cancer initiation and progression. RNF141 is a member of RNFs family; however, its clinical significance, roles, and mechanism in colorectal cancer (CRC) remain poorly understood. Here, we examined the expression of RNF141 in 64 pairs of CRC and adjacent normal tissues by real-time PCR, Western blot, and immunohistochemical analysis. We found that there was more expression of RNF141 in CRC tissue compared with its adjacent normal tissue and high RNF141 expression associated with T stage. In vivo and in vitro functional experiments were conducted and revealed the oncogenic role of RNF141 in CRC. RNF141 knockdown suppressed proliferation, arrested the cell cycle in the G1 phase, inhibited migration, invasion and HUVEC tube formation but promoted apoptosis, whereas RNF141 overexpression exerted the opposite effects in CRC cells. The subcutaneous xenograft models showed that RNF141 knockdown reduced tumor growth, but its overexpression promoted tumor growth. Mechanistically, liquid chromatography-tandem mass spectrometry indicated RNF141 interacted with KRAS, which was confirmed by Co-immunoprecipitation, Immunofluorescence assay. Further analysis with bimolecular fluorescence complementation (BiFC) and Glutathione-S-transferase (GST) pull-down assays showed that RNF141 could directly bind to KRAS. Importantly, the upregulation of RNF141 increased GTP-bound KRAS, but its knockdown resulted in a reduction accordingly. Next, we demonstrated that RNF141 induced KRAS activation via increasing its enrichment on the plasma membrane not altering total KRAS expression, which was facilitated by the interaction with LYPLA1. Moreover, KRAS silencing partially abolished the effect of RNF141 on cell proliferation and apoptosis. In addition, our findings presented that RNF141 functioned as an oncogene by upregulating KRAS activity in a manner of promoting KRAS enrichment on the plasma membrane in CRC.

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Phosphorylation of the (Na,K)-ATPase by a plasma membrane-bound protein kinase in friend erythroleukemia cells.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)32450-5 ◽

1983 ◽

Vol 258 (10) ◽

pp. 6567-6574 ◽

Cited By ~ 6

Author(s):

L A Yeh ◽

L Ling ◽

L English ◽

L Cantley

Keyword(s):

Plasma Membrane ◽

Protein Kinase ◽

Erythroleukemia Cells ◽

Membrane Bound ◽

Friend Erythroleukemia Cells

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Craniofacial Diseases Caused by Defects in Intracellular Trafficking

Genes ◽

10.3390/genes12050726 ◽

2021 ◽

Vol 12 (5) ◽

pp. 726

Author(s):

Chung-Ling Lu ◽

Jinoh Kim

Keyword(s):

Endoplasmic Reticulum ◽

Membrane Proteins ◽

Intracellular Trafficking ◽

Critical Role ◽

Treatment Strategies ◽

Soluble Proteins ◽

Genes Encoding ◽

Membrane Bound ◽

Signaling Receptors ◽

Craniofacial Morphogenesis

Cells use membrane-bound carriers to transport cargo molecules like membrane proteins and soluble proteins, to their destinations. Many signaling receptors and ligands are synthesized in the endoplasmic reticulum and are transported to their destinations through intracellular trafficking pathways. Some of the signaling molecules play a critical role in craniofacial morphogenesis. Not surprisingly, variants in the genes encoding intracellular trafficking machinery can cause craniofacial diseases. Despite the fundamental importance of the trafficking pathways in craniofacial morphogenesis, relatively less emphasis is placed on this topic, thus far. Here, we describe craniofacial diseases caused by lesions in the intracellular trafficking machinery and possible treatment strategies for such diseases.

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PROBLEMS ASSOCIATED WITH THE DEMONSTRATION BY LEAD METHODS OF ADENOSINE TRIPHOSPHATASE ACTIVITY IN RESIDENT PERITONEAL MACROPHAGES AND EXUDATE MONOCYTES OF THE GUINEA PIG

Journal of Histochemistry & Cytochemistry ◽

10.1177/21.5.488 ◽

1973 ◽

Vol 21 (5) ◽

pp. 488-498 ◽

Cited By ~ 16

Author(s):

R. E. POELMANN ◽

W. T. DAEMS ◽

E. J. VAN LOHUIZEN

Keyword(s):

Plasma Membrane ◽

Guinea Pig ◽

Microscopic Study ◽

Heterogeneous Nucleation ◽

Adenosine Triphosphatase ◽

Peritoneal Macrophages ◽

Electron Microscopic ◽

Adenosine Triphosphatase Activity ◽

Eosinophilic Granulocytes ◽

Membrane Bound

This cytochemical and electron microscopic study on peritoneal macrophages of the guinea pig has raised doubts concerning the validity of lead methods for the demonstration of plasma membrane-bound adenosine triphosphatase activity. The problems encountered are inherent in the use of lead ions as a capture reagent. The nonenzymatically formed precipitates reflect sites of heterogeneous nucleation specific for certain kinds of cells, e.g., resident peritoneal macrophages, eosinophilic granulocytes and, to a lesser degree, exudate monocytes. This type of precipitation is also catalyzed on the surface of nonbiologic matrices such as latex particles. Enzymatic processes may well occur, but they cannot be distinguished from nonenzymatic processes.

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