VAM-1: a new member of the MAGUK family binds to human Veli-1 through a conserved domain

Tseng, Joseph T.; Marfatia, Shirin M.; Bryant, Peter J.; Pack, Svetlana D.; Zhuang, Zhenping; O’Brien, Jonathan E.; Lin, Lunhui; Hanada, Toshihiko; Chishti, Athar H.

doi:10.1016/s0167-4781(01)00191-9

Cited by 37 publications

(29 citation statements)

References 28 publications

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“…Thus, it became clear that 4.1G does not seem to be the only protein to anchor CADM1 at cell membranes of germ cells, and the membrane skeletal complex in Sertoli and germ cells seems to be much larger than we expected. Membraneassociated guanylate kinase homolog (MAGUK) proteins, such as the p55 family identified in erythrocytes and renal proximal tubules of mice (Tseng et al 2001, Terada et al 2007, interacting with the 4.1-family proteins, may be another carrier of CADM1 into cell membranes because it has some domains attaching to the MAGUK proteins (Wakayama & Iseki 2009). Further examination to find such a molecular complex is necessary to determine functional relevance of membrane skeletons including 4.1-family proteins in seminiferous tubules, and also analyses of CADM1-deficient seminiferous tubules may help to understand the membrane skeletal complex.…”

Section: Discussionmentioning

confidence: 99%

Involvement of a membrane skeletal protein, 4.1G, for Sertoli/germ cell interaction

Terada¹,

Ohno²,

Saitoh³

et al. 2010

Reproduction

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We previously reported that a membrane skeletal protein, 4.1G (also known as EPB41L2), is immunolocalized in mouse seminiferous tubules. In this study, the 4.1G immunolocalizaiton was precisely evaluated at various stages of the mouse seminiferous epithelial cycle with 'in vivo cryotechnique' and also with pre-embedding immunoelectron microscopy in testicular tissues whose ultrastructures were well preserved with glycerol treatment before cryosectioning. In addition, 4.1G-deficient mice were produced, and the morphology of their seminiferous tubules was also evaluated. The 4.1G immunolocalization was different among stages, indicating that it was not only along cell membranes of Sertoli cells, but also those of spermatogonia and early spermatocytes. To confirm the 4.1G immunolocalization in germ cells, in vitro culture of spermatogonial stem cells (SSCs) was used for immunocytochemistry and immunoblotting analysis. In the cultured SSCs, 4.1G was clearly expressed and immunolocalized along cell membranes, especially at mutual attaching regions. In testicular tissues, cell adhesion molecule-1 (CADM1), an intramembranous adhesion molecule, was colocalized on basal parts of the seminiferous tubules and immunoprecipitated with 4.1G in the tissue lysate. Interestingly, in the 4.1G-deficient mice, histological manifestation of the seminiferous tubules was not different from that in wild-type mice, and the CADM1 was also immunolocalized in the same pattern as that in the wild-type. Moreover, the 4.1G-deficient male mice were fertile. These results were probably due to functional redundancy of unknown membrane skeletal molecules in germ cells. Thus, a novel membrane skeletal protein, 4.1G, was found in germ cells, and considering its interaction with CADM family, it probably has roles in attachment of both Sertoli-germ and germ-germ cells.

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Section: Discussionmentioning

confidence: 99%

Involvement of a membrane skeletal protein, 4.1G, for Sertoli/germ cell interaction

Terada¹,

Ohno²,

Saitoh³

et al. 2010

Reproduction

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“…The interaction with protein 4.1N was not abolished in the CASK mutant, indicating that other residues in the HOOK region are participating. Notably, this tetralysine motif is present in several MAGUK proteins but alone is not sufficient to confer protein 4.1 binding (39). Importantly, actin and spectrin were immobilized concomitantly to protein 4.1 on CASK.…”

Section: Figmentioning

confidence: 99%

CASK and Protein 4.1 Support F-actin Nucleation on Neurexins

Biederer

Südhof

2001

Journal of Biological Chemistry

162

128

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Rearrangements of the actin cytoskeleton are involved in a variety of cellular processes from locomotion of cells to morphological alterations of the cell surface. One important question is how local interactions of cells with the extracellular space are translated into alterations of their membrane organization. To address this problem, we studied CASK, a member of the membraneassociated guanylate kinase homologues family of adaptor proteins. CASK has been shown to bind the erythrocyte isoform of protein 4.1, a class of proteins that promote formation of actin/spectrin microfilaments. In neurons, CASK also interacts via its PDZ domain with the cytosolic C termini of neurexins, neuron-specific cell-surface proteins. We now show that CASK binds a brain-enriched isoform of protein 4.1, and nucleates local assembly of actin/spectrin filaments. These interactions can be reconstituted on the cytosolic tail of neurexins. Furthermore, CASK can be recovered with actin filaments prepared from rat brain extracts, and neurexins are recruited together with CASK and protein 4.1 into these actin filaments. Thus, analogous to the PDZdomain protein p55 and glycophorin C at the erythrocyte membrane, a similar complex comprising CASK and neurexins exists in neurons. Our data suggest that intercellular junctions formed by neurexins, such as junctions initiated by ␤-neurexins with neuroligins, are at least partially coupled to the actin cytoskeleton via an interaction with CASK and protein 4

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“…Homologs of LIN-2, LIN-7, and LIN-10 have also been identified in mammals; they are called CASK/PALS, VELI/MALS, and MINT/X11, respectively (13)(14)(15)(16)(17)(18)(19)(20). These proteins have been observed in most neuronal and epithelial cell types and form a variety of dimeric or trimeric complexes (13,(21)(22)(23)(24)(25).…”

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confidence: 99%

Coordinated Folding and Association of the LIN-2, -7 (L27) Domain

Harris¹,

Venkatasubrahmanyam²,

Lim

2002

Journal of Biological Chemistry

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LIN-2, -7 (L27) homology domains are putative protein-protein interaction modules found in several scaffold proteins involved in the assembly of polarized cellsignaling structures. These specific interaction pairs are well conserved across metazoan species, from worms to man. We have expressed and purified L27 domains from multiple species and find that certain domains from proteins such as Caenorhabditis elegans LIN-2 and LIN-7 can specifically heterodimerize. Biophysical analysis of interacting L27 domains demonstrates that the domains interact with a 1:1 stoichiometry. Circular dichroism studies reveal that the domains appear to function as an obligate heterodimer; individually the domains are largely unfolded, but when associated they show a significant increase in helicity, as well as a cooperative unfolding transition. These novel obligate interacting pairs are likely to play a key role in regulating the organization of signaling proteins at polarized cell structures.

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VAM-1: a new member of the MAGUK family binds to human Veli-1 through a conserved domain

Cited by 37 publications

References 28 publications

Involvement of a membrane skeletal protein, 4.1G, for Sertoli/germ cell interaction

Involvement of a membrane skeletal protein, 4.1G, for Sertoli/germ cell interaction

CASK and Protein 4.1 Support F-actin Nucleation on Neurexins

Coordinated Folding and Association of the LIN-2, -7 (L27) Domain

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