PICK1 inhibition of the Arp2/3 complex controls dendritic spine size and synaptic plasticity

Nakamura, Yasuko; Wood, Catherine L.; Patton, Andrew P.; Jaafari, Nadia; Henley, Jeremy M.; Mellor, Jack R.; Hanley, Jonathan G.

doi:10.1038/emboj.2010.357

Cited by 90 publications

(88 citation statements)

References 39 publications

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“…Additionally, PICK1 was reported to interact with F-actin and the Arp2/3 complex and to act as a suppressor of WASP-and WAVEmediated Arp2/3 complex activation (Rocca et al, 2008). In line with this, PICK1 knockdown does not phenocopy the Arp2/3 complex loss-of-function, but instead leads to an increase in spine size (Nakamura et al, 2011). The inhibitory effect of PICK1 on Arp2/3 complex-mediated actin nucleation can be released by the interaction of the small GTPase Arf1 with PICK1, and is considered an important mechanism in PICK1-mediated endocytosis of AMPA…”

Section: The Power Of Physical Integrationsupporting

confidence: 54%

Different functional modes of BAR domain proteins in formation and plasticity of mammalian postsynapses

Kessels

Qualmann

2015

Journal of Cell Science

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A plethora of cell biological processes involve modulations of cellular membranes. By using extended lipid-binding interfaces, some proteins have the power to shape membranes by attaching to them. Among such membrane shapers, the superfamily of Bin–Amphiphysin–Rvs (BAR) domain proteins has recently taken center stage. Extensive structural work on BAR domains has revealed a common curved fold that can serve as an extended membrane-binding interface to modulate membrane topologies and has allowed the grouping of the BAR domain superfamily into subfamilies with structurally slightly distinct BAR domain subtypes (N-BAR, BAR, F-BAR and I-BAR). Most BAR superfamily members are expressed in the mammalian nervous system. Neurons are elaborately shaped and highly compartmentalized cells. Therefore, analyses of synapse formation and of postsynaptic reorganization processes (synaptic plasticity) – a basis for learning and memory formation – has unveiled important physiological functions of BAR domain superfamily members. These recent advances, furthermore, have revealed that the functions of BAR domain proteins include different aspects. These functions are influenced by the often complex domain organization of BAR domain proteins. In this Commentary, we review these recent insights and propose to classify BAR domain protein functions into (1) membrane shaping, (2) physical integration, (3) action through signaling components, and (4) suppression of other BAR domain functions.

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Section: The Power Of Physical Integrationsupporting

confidence: 54%

Different functional modes of BAR domain proteins in formation and plasticity of mammalian postsynapses

Kessels

Qualmann

2015

Journal of Cell Science

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“…It is conceivable that the actin cytoskeleton at this age is already at a depolymerized or dynamic state, and therefore further activation of cofilin is no longer needed to induce actin reorganization. Alternatively, other actin regulators such as Arp2/3 complex known to be regulated by PICK1 (Rocca et al, 2008;Nakamura et al, 2011;Rocca et al, 2013) may function to mediate actin change at the young synapse. Further experiments will be needed to elucidate how cofilin and Arp2/3 interact to regulate LTD during developmental maturation.…”

Section: Discussionmentioning

confidence: 99%

Developmental regulation of hippocampal long-term depression by cofilin-mediated actin reorganization

et al. 2017

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“…PICK1 shRNA, WT-PICK1, DD4,6AA-PICK1 and ⌬380 -390 -PICK1 (previously referred to as ⌬CT-PICK1) have been reported previously (Hanley and Henley, 2005;Nakamura et al, 2011). cDNA encoding mCherry-PICK1 was ligated into pCDNA3.1.…”

Section: Methodsmentioning

confidence: 99%

“…We first used shRNA to reduce endogenous PICK1 expression (Nakamura et al, 2011) and analyzed GluA2 surface expression at a range of time points after glycine treatment. As presented in Figure 1 B, GluA2 trafficking to the cell surface in control neurons expressing EGFP is delayed until 10 min after glycine stimulus and continues to increase until 20 min after stimulus.…”

Section: Delayed Insertion Of Glua2 After Glycine Stimulation Is Pickmentioning

confidence: 99%

PICK1 Mediates Transient Synaptic Expression of GluA2-Lacking AMPA Receptors during Glycine-Induced AMPA Receptor Trafficking

2012

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The number and subunit composition of postsynaptic AMPA receptors (AMPARs) is a key determinant of synaptic transmission. The vast majority of AMPARs contain GluA2 subunit, which renders the channel impermeable to calcium. However, a small proportion are GluA2 lacking and therefore calcium permeable (CP-AMPARs). It has been proposed recently that long-term potentiation (LTP) involves not only an increase in the total number of AMPARs at the synapse but also a transient switch to CP-AMPARs in the first few minutes after LTP induction. The molecular mechanisms that underlie this switch to CP-AMPARs and the subsequent switch back to calciumimpermeable AMPARs are unknown. Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. In contrast, GluA2 is restricted from trafficking to the cell surface by a glycine-induced increase in PICK1-GluA2 binding on endosomal compartments. Between 5 and 20 min after stimulus, activation of CP-AMPARs triggers a release of GluA2 from PICK1, allowing GluA2-containing AMPARs to traffic to the synaptic plasma membrane. These results define a PICK1-dependent mechanism that underlies transient alterations in the subunit composition and calcium permeability of synaptic AMPARs that is important during the early phase after stimulation with glycine and therefore is likely to be important during the expression of LTP.

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PICK1 inhibition of the Arp2/3 complex controls dendritic spine size and synaptic plasticity

Abstract: Dendritic spine remodelling involves regulated actin dynamics and is essential for synaptic plasticity. The Arp2/3 inhibitor PICK1 is here shown to regulate spine size: inducing shrinkage during long-term depression.

Cited by 90 publications

References 39 publications

Different functional modes of BAR domain proteins in formation and plasticity of mammalian postsynapses

Different functional modes of BAR domain proteins in formation and plasticity of mammalian postsynapses

Developmental regulation of hippocampal long-term depression by cofilin-mediated actin reorganization

PICK1 Mediates Transient Synaptic Expression of GluA2-Lacking AMPA Receptors during Glycine-Induced AMPA Receptor Trafficking

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