scholarly journals PRA Isoforms Are Targeted to Distinct Membrane Compartments

2000 ◽  
Vol 276 (9) ◽  
pp. 6225-6233 ◽  
Author(s):  
Mohammad Abdul-Ghani ◽  
Pierre-Yves Gougeon ◽  
Derek C. Prosser ◽  
Lance F. Da-Silva ◽  
Johnny K. Ngsee
Keyword(s):  
Membrane Compartments ◽  
Distinct Membrane

Targeting Rab GTPases to distinct membrane compartments

2004 ◽  
Vol 5 (11) ◽  
pp. 886-896 ◽  
Author(s):  
Suzanne Pfeffer ◽  
Dikran Aivazian
Keyword(s):  
Rab Gtpases ◽  
Membrane Compartments ◽  
Distinct Membrane

scholarly journals Differential regulation of adipocyte PDE3B in distinct membrane compartments in response to insulin and CL316243

2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Faiyaz Ahmad Khan ◽  
Rebecka Lindh ◽  
Yan Tang ◽  
Lida Ruishalme ◽  
Anita Ost ◽  
...  
Keyword(s):  
Differential Regulation ◽  
Membrane Compartments ◽  
Distinct Membrane

scholarly journals TIP47 is a key effector for Rab9 localization

2006 ◽  
Vol 173 (6) ◽  
pp. 917-926 ◽  
Author(s):  
Dikran Aivazian ◽  
Ramon L. Serrano ◽  
Suzanne Pfeffer
Keyword(s):  
Steady State ◽  
Human Genome ◽  
Effector Proteins ◽  
Rab Gtpases ◽  
Interacting Protein ◽  
Cellular Concentration ◽  
Membrane Compartments ◽  
Effector Binding ◽  
Distinct Membrane

The human genome encodes ∼70 Rab GTPases that localize to the surfaces of distinct membrane compartments. To investigate the mechanism of Rab localization, chimeras containing heterologous Rab hypervariable domains were generated, and their ability to bind seven Rab effectors was quantified. Two chimeras could bind effectors for two distinctly localized Rabs; a Rab5/9 hybrid bound both Rab5 and Rab9 effectors, and a Rab1/9 hybrid bound to certain Rab1 and Rab9 effectors. These unusual chimeras permitted a test of the importance of effector binding for Rab localization. In both cases, changing the cellular concentration of a key Rab9 effector, which is called tail-interacting protein of 47 kD, moved a fraction of the proteins from their parental Rab localization to that of Rab9. Thus, relative concentrations of certain competing effectors could determine a chimera's localization. These data confirm the importance of effector interactions for Rab9 localization, and support a model in which effector proteins rely on Rabs as much as Rabs rely on effectors to achieve their correct steady state localizations.

The spectrin-based membrane skeleton as a membrane protein-sorting machine

1996 ◽  
Vol 270 (5) ◽  
pp. C1263-C1270 ◽  
Author(s):  
K. A. Beck ◽  
W. J. Nelson
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Cell Function ◽  
Protein Sorting ◽  
Membrane Skeleton ◽  
Membrane Domains ◽  
Sorting Machine ◽  
Membrane Compartments ◽  
Molecular Machinery ◽  
Distinct Membrane

Normal cell function is dependent on the existence of membrane compartments that have unique populations of membrane proteins. Sorting of membrane proteins forms the basis for the biogenesis of distinct membrane compartments. There are many examples of membrane protein-sorting events in cells, but the molecular machinery involved is poorly understood. We discuss characteristics of a putative membrane protein-sorting machine and show that the spectrin-based membrane skeleton conforms to these characteristics. The spectrin-based membrane skeleton is a submembranous, spatially limited, two-dimensional lattice that binds a subset of membrane proteins. These properties allow the membrane skeleton to facilitate the formation of distinct membrane domains and thus reveal its potential as a membrane protein-sorting machine.

scholarly journals Membrane association but not identity is required for LRRK2 activation and phosphorylation of Rab GTPases

2019 ◽  
Vol 218 (12) ◽  
pp. 4157-4170 ◽  
Author(s):  
Rachel C. Gomez ◽  
Paulina Wawro ◽  
Pawel Lis ◽  
Dario R. Alessi ◽  
Suzanne R. Pfeffer
Keyword(s):  
Plasma Membrane ◽  
Cell Biology ◽  
Family Members ◽  
Membrane Association ◽  
Rab Gtpases ◽  
Membrane Compartments ◽  
Membrane Bound ◽  
Lrrk2 Kinase ◽  
Familial Parkinson’S Disease ◽  
Distinct Membrane

LRRK2 kinase mutations cause familial Parkinson’s disease and increased phosphorylation of a subset of Rab GTPases. Rab29 recruits LRRK2 to the trans-Golgi and activates it there, yet some of LRRK2’s major Rab substrates are not on the Golgi. We sought to characterize the cell biology of LRRK2 activation. Unlike other Rab family members, we show that Rab29 binds nucleotide weakly, is poorly prenylated, and is not bound to GDI in the cytosol; nevertheless, Rab29 only activates LRRK2 when it is membrane bound and GTP bound. Mitochondrially anchored, GTP-bound Rab29 is both a LRRK2 substrate and activator, and it drives accumulation of active LRRK2 and phosphorylated Rab10 on mitochondria. Importantly, mitochondrially anchored LRRK2 is much less capable of phosphorylating plasma membrane–anchored Rab10 than soluble LRRK2. These data support a model in which LRRK2 associates with and dissociates from distinct membrane compartments to phosphorylate Rab substrates; if anchored, LRRK2 can modify misdelivered Rab substrates that then become trapped there because GDI cannot retrieve them.

scholarly journals Seven Novel Mammalian SNARE Proteins Localize to Distinct Membrane Compartments

1998 ◽  
Vol 273 (17) ◽  
pp. 10317-10324 ◽  
Author(s):  
Raj J. Advani ◽  
Hae-Rahn Bae ◽  
Jason B. Bock ◽  
Daniel S. Chao ◽  
Yee-Cheen Doung ◽  
...  
Keyword(s):  
Snare Proteins ◽  
Membrane Compartments ◽  
Distinct Membrane

Calcium ion imaging in plant cells

1993 ◽  
Vol 51 ◽  
pp. 132-133
Author(s):  
Peter K. Hepler ◽  
Dale A. Callaham
Keyword(s):  
Plant Cell Wall ◽  
Cytoplasmic Membrane ◽  
Fluorescent Dyes ◽  
Free Acid ◽  
Methyl Esters ◽  
Free Calcium ◽  
Local Concentration ◽  
Ion Imaging ◽  
Membrane Compartments ◽  
Free Acid Form

Calcium ions (Ca) participate in many signal transduction processes, and for that reason it is important to determine where these ions are located within the living cell, and when and to what extent they change their local concentration. Of the different Ca-specific indicators, the fluorescent dyes, developed by Grynkiewicz et al. (1), have proved most efficacious, however, their use on plants has met with several problems (2). First, the dyes as acetoxy-methyl esters are often cleaved by extracellular esterases in the plant cell wall, and thus they do not enter the cell. Second, if the dye crosses the plasma membrane it may continue into non-cytoplasmic membrane compartments. Third, even if cleaved by esterases in the cytoplasm, or introduced as the free acid into the cytoplasmic compartment, the dyes often become quickly sequestered into vacuoles and organelles, or extruded from the cell. Finally, the free acid form of the dye readily complexes with proteins reducing its ability to detect free calcium. All these problems lead to an erroneous measurement of calcium (2).

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