Organization and regulation of proteins at synapses

407

Erratum Organization

and regulation

of proteins

at synapses

Jee Hae Kim and Richard L Huganir Current

Opinion

in Cell Biology

1999,

11:248-254

http://biomednet.com/elecref/0955067401100246 ic Elsevier

Science

Ltd

ISSN

0955-0674

The publishers wish to state that Figure 1 and Figure 2 were transposed. Figures 1 and 2 follow with the correct legends.

Figure

1

NMDAR

AMPAR

PSD-95/SAP90

Current Opinm A schematic diagram of a synaptic junction with pre- and postsynaptic macromolecular complexes. The presynaptic terminal is poised to deliver glutamate to the synaptic cleft and the PDZ domain containing proteins, CASKILIN-2, Mint1 /LIN-10, and VeWLIN-7 are in a complex and may recruit more proteins necessary for the presynaptic specialization. Intercellular junctions may be stabilized by the interaction between the presynaptic P-neurexin and the postsynaptic neuroligin. Postsynaptic glutamate receptors are clustered In association with

m Cell B~oloav

PDZ-domatn containing proteins. NMDA receptors (NMDAR) are in association with PSD-95/SAP90 and SAP1 02 that interact with GKAPSAPAP, nNOS, and SynGAP. AMPA receptors (AMPAR) are similarly organized with GRIP1 and 2, PlCKl, and ABP These proteins may act to localize the receptors, affect the receptor function, and to transduce the signals that are initiated postsynaptically. NSF is shown with subsurface AMPA receptors in vesicles and may be involved in the regulated membrane insertion of AMPA receptors.

~

408

Figure

Cell regulation

2

The synaptic targeting of glutamate receptors involves the transport of the receptors in vesicles to the dendrites followed by regulated membrane fusion events. The receptors may be stabilized and/or modified their function by kinases in the cytoskeletal network in the postsynaptic density. The receptors are then subjected to endocytosis regulating the receptor density on the postsynaptic surface. The cycling of the receptors may be modulated by various cellular pathways such as the protern phosphorylation by PKC, PKA, CaMKll PTK, and by Ras and second messenger signaling cascades.

in

and

Current

Op~nton I” Cell