PICK1 regulates AMPA receptor endocytosis via direct interactions with AP2 α-appendage and dynamin

Fiuza, María; Rostosky, Christine M.; Parkinson, Gabrielle T.; Bygrave, Alexei M.; Halemani, Nagaraj D.; Baptista, Márcio S.; Milošević, Ira; Hanley, Jonathan G.

doi:10.1083/jcb.201701034

Cited by 57 publications

(70 citation statements)

References 62 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recently, PICK1 was also shown to interact with a central player in clathrin-mediated endocytosis, the adaptor protein AP2, which bridges cargo proteins and clathrin. This interaction is required for AMPAR clustering and internalization upon NDMAR stimulation [ 133 ].…”

Section: Pdz Domain-containing Interactantsmentioning

confidence: 99%

AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking

Bissen

Foss

Acker‐Palmer

2019

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

To correctly transfer information, neuronal networks need to continuously adjust their synaptic strength to extrinsic stimuli. This ability, termed synaptic plasticity, is at the heart of their function and is, thus, tightly regulated. In glutamatergic neurons, synaptic strength is controlled by the number and function of AMPA receptors at the postsynapse, which mediate most of the fast excitatory transmission in the central nervous system. Their trafficking to, at, and from the synapse, is, therefore, a key mechanism underlying synaptic plasticity. Intensive research over the last 20 years has revealed the increasing importance of interacting proteins, which accompany AMPA receptors throughout their lifetime and help to refine the temporal and spatial modulation of their trafficking and function. In this review, we discuss the current knowledge about the roles of key partners in regulating AMPA receptor trafficking and focus especially on the movement between the intracellular, extrasynaptic, and synaptic pools. We examine their involvement not only in basal synaptic function, but also in Hebbian and homeostatic plasticity. Included in our review are well-established AMPA receptor interactants such as GRIP1 and PICK1, the classical auxiliary subunits TARP and CNIH, and the newest additions to AMPA receptor native complexes.

show abstract

Section: Pdz Domain-containing Interactantsmentioning

confidence: 99%

AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking

Bissen

Foss

Acker‐Palmer

2019

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

show abstract

“…In addition, PICK1 was also able to promote dynamin polymerization by interacting with its GTPase domain. This work interestingly suggests that PICK1 not only links AMPA-Rs to the endocytic machinery to enhance its internalization but that it is directly able to promote the activity of two crucial players in endocytosis events, AP-2 and dynamin (Fiuza et al, 2017 ).…”

Section: Synaptic Plasticitymentioning

confidence: 99%

“…Recently, Fiuza et al ( 2017 ) further elucidated the mechanism through which PICK1 mediates GluA2 removal from the surface membrane. The authors showed that PICK1 is recruited to clathrin-coated pits by interacting with the adaptor protein complex AP-2, an association enhanced by LTD-like NMDA-R activation.…”

Section: Synaptic Plasticitymentioning

confidence: 99%

Recent Findings on AMPA Receptor Recycling

Moretto

Passafaro

2018

Front. Cell. Neurosci.

View full text Add to dashboard Cite

α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPA-Rs) are tetrameric protein complexes that mediate most of the fast-excitatory transmission in response to the neurotransmitter glutamate in neurons. The abundance of AMPA-Rs at the surface of excitatory synapses establishes the strength of the response to glutamate. It is thus evident that neurons need to tightly regulate this feature, particularly in the context of all synaptic plasticity events, which are considered the biological correlates of higher cognitive functions such as learning and memory. AMPA-R levels at the synapse are regulated by insertion of newly synthesized receptors, lateral diffusion on the plasma membrane and endosomal cycling. The latter is likely the most important especially for synaptic plasticity. This process starts with the endocytosis of the receptor from the cell surface and is followed by either degradation, if the receptor is directed to the lysosomal compartment, or reinsertion at the cell surface through a specialized endosomal compartment called recycling endosomes. Although the basic steps of this process have been discovered, the details and participation of additional regulatory proteins are still being discovered. In this review article, we describe the most recent findings shedding light on this crucial mechanism of synaptic regulation.

show abstract

“…(Praefcke et al, 2004 ; Daumke et al, 2014 ; Suetsugu et al, 2014 ). A recent addition to the BAR domain proteins identified as an α-appendage interactor is protein interacting with C-Kinase 1 (PICK1; Figure 1B ; Fiuza et al, 2017 ), which has a well-established role in decreasing the surface and synaptic levels of GluA2-containing AMPARs (Terashima et al, 2004 ). The PICK1 PDZ domain binds the C-terminal tail of AMPAR subunit GluA2, and disrupting this interaction with competing peptides or by mutagenesis inhibits both constitutive and NMDAR-stimulated AMPAR internalization and LTD in hippocampal neurons (Daw et al, 2000 ; Osten et al, 2000 ; Iwakura et al, 2001 ), as well as cerebellar LTD.…”

Section: Early Stages Of Clathrin-coated Pit Formationmentioning

confidence: 99%

“…PICK1 binds directly to AP2 with similar consensus motifs (FxDxF and DxF) to numerous other endocytic accessory proteins (Praefcke et al, 2004 ; Olesen et al, 2008 ; Fiuza et al, 2017 ). Mutating the critical aspartate residues to alanines in PICK1 disrupts AP2 binding and consequently inhibits both constitutive and NMDAR-dependent internalization of endogenous GluA2-containing AMPARs (Fiuza et al, 2017 ).…”

Section: Early Stages Of Clathrin-coated Pit Formationmentioning

confidence: 99%

The Regulation of AMPA Receptor Endocytosis by Dynamic Protein-Protein Interactions

Hanley

2018

Front. Cell. Neurosci.

Self Cite

View full text Add to dashboard Cite

The precise regulation of AMPA receptor (AMPAR) trafficking in neurons is crucial for excitatory neurotransmission, synaptic plasticity and the consequent formation and modification of neural circuits during brain development and learning. Clathrin-mediated endocytosis (CME) is an essential trafficking event for the activity-dependent removal of AMPARs from the neuronal plasma membrane, resulting in a reduction in synaptic strength known as long-term depression (LTD). The regulated AMPAR endocytosis that underlies LTD is caused by specific modes of synaptic activity, most notably stimulation of NMDA receptors (NMDARs) and metabotropic glutamate receptors (mGluRs). Numerous proteins associate with AMPAR subunits, directly or indirectly, to control their trafficking, and therefore the regulation of these protein-protein interactions in response to NMDAR or mGluR signaling is a critical feature of synaptic plasticity. This article reviews the protein-protein interactions that are dynamically regulated during synaptic plasticity to modulate AMPAR endocytosis, focussing on AMPAR binding proteins and proteins that bind the core endocytic machinery. In addition, the mechanisms for the regulation of protein-protein interactions are considered, as well as the functional consequences of these dynamic interactions on AMPAR endocytosis.

show abstract

PICK1 regulates AMPA receptor endocytosis via direct interactions with AP2 α-appendage and dynamin

Cited by 57 publications

References 62 publications

AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking

AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking

Recent Findings on AMPA Receptor Recycling

The Regulation of AMPA Receptor Endocytosis by Dynamic Protein-Protein Interactions

Contact Info

Product

Resources

About