Chapter 7 Compartmentalizing the Neuronal Plasma Membrane

Lasiecka, Zofia M.; Yap, Chan Choo; Vakulenko, Max; Winckler, Bettina

doi:10.1016/s1937-6448(08)01607-9

Cited by 43 publications

(28 citation statements)

References 435 publications

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“…The analysis of these developmental phenomena is in its infancy. We know of many proteins that are differentially expressed in specific membrane domains [59],[60] and that the directional protein transport in axons and dendrites is controlled by different mechanisms. However, the exact mechanisms of targeted protein expression are unknown.…”

Section: Discussionmentioning

confidence: 99%

An Integrated Micro- and Macroarchitectural Analysis of the Drosophila Brain by Computer-Assisted Serial Section Electron Microscopy

et al. 2010

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Section: Discussionmentioning

confidence: 99%

An Integrated Micro- and Macroarchitectural Analysis of the Drosophila Brain by Computer-Assisted Serial Section Electron Microscopy

et al. 2010

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“…4. Finally some proteins are targeted through transcytosis, in which the protein is first expressed in one compartment from which it is removed by endocytosis and then shipped to the appropriate locale through recycling endosomes (Lasiecka et al, 2009). …”

Section: Discussionmentioning

confidence: 99%

TRIP8b Splice Forms Act in Concert to Regulate the Localization and Expression of HCN1 Channels in CA1 Pyramidal Neurons

Piskorowski

Santoro

Siegelbaum

2011

Neuron

107

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Summary HCN1 channel subunits, which contribute to the hyperpolarization-activated cation current (Ih), are selectively targeted to distal apical dendrites of hippocampal CA1 pyramidal neurons. Here we addressed the importance of the brain-specific auxiliary subunit of HCN1, TRIP8b, in regulating HCN1 expression and localization. More than ten N-terminal splice variants of TRIP8b exist in brain and exert distinct effects on HCN1 trafficking when overexpressed. We found that isoform-wide disruption of the TRIP8b/HCN1 interaction caused HCN1 to be mistargeted throughout CA1 somatodendritic compartments. In contrast, HCN1 was targeted normally to CA1 distal dendrites in a TRIP8b knockout mouse that selectively lacked exons 1b and 2. Of the two remaining hippocampal TRIP8b isoforms, TRIP8b(1a-4) promoted HCN1 surface expression in dendrites whereas TRIP8b(1a) suppressed HCN1 misexpression in axons. Thus, proper subcellular localization of HCN1 depends on its differential additive and subtractive sculpting by two isoforms of a single auxiliary subunit gene.

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“…PI(4,5)P 2 and PI(3,4,5)P 3 are enriched in plasma membrane with 16:0/18:1, 18:0/20:4, and 18:0/22:6 isoforms predominating (Igbavboa et al, 2002). PI(4)P is found more frequently in Golgi membranes while PI(3)P and PI(3,5)P 2 are enriched in endosomal membranes (Lasiecka et al, 2009). In yeast, PI(3)P both enhances the capacity of membrane-bound SNARES to drive fusion in the absence of SNARE chaperones as well as synergistically activates SNARE chaperones to recruit Vam7p into fusion-competent complexes.…”

Section: Pattern 2: Breakdown Of the Second Messenger Glycerophospholmentioning

confidence: 99%

Using neurolipidomics to identify phospholipid mediators of synaptic (dys)function in Alzheimer's Disease

Bennett¹,

Valenzuela²,

Xu³

et al. 2013

Front. Physiol.

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Not all of the mysteries of life lie in our genetic code. Some can be found buried in our membranes. These shells of fat, sculpted in the central nervous system into the cellular (and subcellular) boundaries of neurons and glia, are themselves complex systems of information. The diversity of neural phospholipids, coupled with their chameleon-like capacity to transmute into bioactive molecules, provides a vast repertoire of immediate response second messengers. The effects of compositional changes on synaptic function have only begun to be appreciated. Here, we mined 29 neurolipidomic datasets for changes in neuronal membrane phospholipid metabolism in Alzheimer's Disease (AD). Three overarching metabolic disturbances were detected. We found that an increase in the hydrolysis of platelet activating factor precursors and ethanolamine-containing plasmalogens, coupled with a failure to regenerate relatively rare alkyl-acyl and alkenyl-acyl structural phospholipids, correlated with disease severity. Accumulation of specific bioactive metabolites [i.e., PC(O-16:0/2:0) and PE(P-16:0/0:0)] was associated with aggravating tau pathology, enhancing vesicular release, and signaling neuronal loss. Finally, depletion of PI(16:0/20:4), PI(16:0/22:6), and PI(18:0/22:6) was implicated in accelerating Aβ42 biogenesis. Our analysis further suggested that converging disruptions in platelet activating factor, plasmalogen, phosphoinositol, phosphoethanolamine (PE), and docosahexaenoic acid metabolism may contribute mechanistically to catastrophic vesicular depletion, impaired receptor trafficking, and morphological dendritic deformation. Together, this analysis supports an emerging hypothesis that aberrant phospholipid metabolism may be one of multiple critical determinants required for Alzheimer disease conversion.

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Chapter 7 Compartmentalizing the Neuronal Plasma Membrane

Cited by 43 publications

References 435 publications

An Integrated Micro- and Macroarchitectural Analysis of the Drosophila Brain by Computer-Assisted Serial Section Electron Microscopy

An Integrated Micro- and Macroarchitectural Analysis of the Drosophila Brain by Computer-Assisted Serial Section Electron Microscopy

TRIP8b Splice Forms Act in Concert to Regulate the Localization and Expression of HCN1 Channels in CA1 Pyramidal Neurons

Using neurolipidomics to identify phospholipid mediators of synaptic (dys)function in Alzheimer's Disease

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