Six <i>cadm</i>/<i>synCAM</i> genes are expressed in the nervous system of developing zebrafish

Pietri, Thomas; Easley-Neal, Courtney; Wilson, Catherine; Washbourne, Philip

doi:10.1002/dvdy.21397

Cited by 25 publications

(26 citation statements)

References 34 publications

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“…In contrast to the widespread expression of Cadm1, the expression of Cadm3 and Cadm4 seems to be restricted to neurons and glial cells [19,30]. Cadm1 and Cadm4 were major components of the Cadm family in neurons [23,32]. binding partner, actin cytoskeleton [7] in this study, these results suggest that MUPP1 may act as an adaptor or a scaffold protein between Cadms and subcellular proteins.…”

Section: Endogenous Interaction Of Mupp1 With Cadm1mentioning

confidence: 46%

“…2B). These results are not surprising in view of the fact that all four Cadms have a class II PDZ-association motif at C-terminal tail [7,23]. As shown in Fig.…”

Section: β-Galactosidase Activity In Liquid Cultures Of Yeastmentioning

confidence: 52%

“…They contain a highly conserved short cytoplasmic tail containing protein-protein interaction domains [7,23]. Therefore, we tested whether MUPP1 also interacts with the other Cadms (Cadm2, Cadm3, and Cadm4) using yeast two-hybrid assay.…”

Section: β-Galactosidase Activity In Liquid Cultures Of Yeastmentioning

confidence: 99%

“…and Cadm4 in neurons Cadm1 is expressed in most epithelia and neuroepithelia, such as lung, liver, dorsal root ganglia, various regions of the central nervous system [23]. In contrast to the widespread expression of Cadm1, the expression of Cadm3 and Cadm4 seems to be restricted to neurons and glial cells [19,30].…”

Section: Endogenous Interaction Of Mupp1 With Cadm1mentioning

confidence: 99%

“…Cadm1, a multifunctional immunoglobulin-like cell adhesion molecule, is involved in cell-cell interaction and the formation and maintenance of epithelial structure [7,23].…”

Section: Endogenous Interaction Of Mupp1 With Cadm1mentioning

confidence: 99%

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Cadms/SynCAMs/Necls/TSLCs Interact with Multi-PDZ Domain Protein MUPP1

Jang¹,

Jeong²,

Choi³

et al. 2014

Journal of Life Science

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Cell adhesion molecules determine the cell-cell binding and the interactions between cells and extracellular signals. Cell-cell junctional complexes, which maintain the structural integrity of tissues, consist of more than 50 proteins including multi-PDZ domain protein 1 (MUPP1). MUPP1 contains 13 postsynaptic density-95/disks large/zonula occludens-1 (PDZ) domains and serves a scaffolding function for transmembrane proteins and cytoskeletal proteins or signaling proteins, but the mechanism how MUPP1 links and stabilizes the juxtamembrane proteins has not yet been elucidated. We used the yeast two-hybrid system to identify proteins that interact with PDZ domains of MUPP1. We found an interaction between MUPP1 and cell adhesion molecule 1 (Cadm1, also known as SynCAM1, Necl-2, or TSLC1). Cadm1 bound to the second PDZ domain of MUPP1. The carboxyl (C)-terminal end of Cadm1 has a type II PDZ-association motif (-Y-F-I) which was essential for the interaction with MUPP1 in the yeast two-hybrid assay. MUPP1 also bound to the C-terminal cytoplasmic tail region of other Cadm family members (Cadm2, Cadm3, and Cadm4). In addition, these protein-protein interactions were observed in the glutathione S-transferase (GST) pull-down assay and by coimmunoprecipitation. Anti-MUPP1 antibody co-immunoprecipitated Cadm1 and Cadm4 with MUPP1 from mouse brain extracts. These results suggest that MUPP1 could mediate interaction between Cadms and cytoskeletal proteins.

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Section: Endogenous Interaction Of Mupp1 With Cadm1mentioning

confidence: 46%

“…2B). These results are not surprising in view of the fact that all four Cadms have a class II PDZ-association motif at C-terminal tail [7,23]. As shown in Fig.…”

Section: β-Galactosidase Activity In Liquid Cultures Of Yeastmentioning

confidence: 52%

Section: β-Galactosidase Activity In Liquid Cultures Of Yeastmentioning

confidence: 99%

Section: Endogenous Interaction Of Mupp1 With Cadm1mentioning

confidence: 99%

“…Cadm1, a multifunctional immunoglobulin-like cell adhesion molecule, is involved in cell-cell interaction and the formation and maintenance of epithelial structure [7,23].…”

Section: Endogenous Interaction Of Mupp1 With Cadm1mentioning

confidence: 99%

See 3 more Smart Citations

Cadms/SynCAMs/Necls/TSLCs Interact with Multi-PDZ Domain Protein MUPP1

Jang¹,

Jeong²,

Choi³

et al. 2014

Journal of Life Science

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Localization of Cadm2a and Cadm3 proteins during development of the zebrafish nervous system

Hunter

Nikolaou

Odermatt

et al. 2011

J of Comparative Neurology

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Members of the Cadm/SynCAM/Necl/IGSF/TSLC family of cell adhesion molecules are known to have diverse functions during development of the nervous system, but information regarding their role during central nervous system (CNS) development in vivo is scarce. The rapid development of a relatively simple nervous system in larval zebrafish makes them a highly tractable model organism for studying gene function during nervous system development. An essential prerequisite for functional studies is a description of protein localization. To address this we have generated subtype-specific antibodies to two members of the zebrafish cell adhesion molecule family: cadm2a and cadm3. Using these novel antibodies we show that cadm3 and cadm2a are expressed throughout the nervous system of larval stage zebrafish. Particularly striking, and largely nonoverlapping expression of cadm2a and cadm3 is observed in the developing retina and spinal cord. Using in vitro binding assays we show that cadm2a and cadm3 bind heterophilically and preferentially to cadm1 and cadm4, respectively. These binding preferences are very similar to those seen for tetrapod Cadms but our study of protein localization suggests novel and diverse functions of cadms during nervous system development.

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Structural organization and function of mouse photoreceptor ribbon synapses involve the immunoglobulin protein synaptic cell adhesion molecule 1

Ribic

Liu

Crair

et al. 2014

J of Comparative Neurology

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Adhesive interactions in the retina instruct the developmental specification of inner retinal layers. However, potential roles of adhesion in the development and function of photoreceptor synapses remain incompletely understood. This contrasts with our understanding of synapse development in the central nervous system (CNS), which can be guided by select adhesion molecules such as the Synaptic Cell Adhesion Molecule 1 (SynCAM 1/CADM1/Nectin-like 2 protein). This immunoglobulin superfamily protein modulates the development and plasticity of classical excitatory synapses. We now show by immuno-electron microscopy and immunoblotting that SynCAM 1 is expressed on mouse rod photoreceptors and their terminals in the outer nuclear and plexiform layers (ONL and OPL) in a developmentally regulated manner. Expression of SynCAM 1 on rods is low in early postnatal stages (P3-P7), but increases after eye opening (P14). In support of functional roles in the photoreceptors, electroretinogram recordings demonstrate impaired responses to light stimulation in SynCAM 1 knockout (KO) mice. In addition, the structural integrity of synapses in the OPL requires SynCAM 1. Quantitative ultrastructural analysis of SynCAM 1 KO retina measured fewer fully assembled, triadic rod ribbon synapses. Further, rod synapse ribbons are shortened in KO mice and protein levels of Ribeye, a major structural component of ribbons, are reduced in SynCAM 1 KO retina. Together, our results implicate SynCAM 1 in the synaptic organization of the rod visual pathway and provide evidence for novel roles of synaptic adhesion in the structural and functional integrity of ribbon synapses.

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Six cadm/synCAM genes are expressed in the nervous system of developing zebrafish

Cited by 25 publications

References 34 publications

Cadms/SynCAMs/Necls/TSLCs Interact with Multi-PDZ Domain Protein MUPP1

Cadms/SynCAMs/Necls/TSLCs Interact with Multi-PDZ Domain Protein MUPP1

Localization of Cadm2a and Cadm3 proteins during development of the zebrafish nervous system

Structural organization and function of mouse photoreceptor ribbon synapses involve the immunoglobulin protein synaptic cell adhesion molecule 1

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