Gap junction and its cytoskeletal undercoats as involved in invagination-endocytosis.

Watanabe, Hiroshi; Washioka, Hiroshi; Tonosaki, Akira

doi:10.1620/tjem.156.175

Cited by 23 publications

(10 citation statements)

References 19 publications

(13 reference statements)

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“…In deeper invaginations of withdrawing GJs, parallel microfilament arrays formed a submembraneous sheath with an orthogonal arrangement toward the long axis of the invagination. These findings imply that the microfilament network and sheath of actin act in concert to generate a mechanical force driving the invagination-endocytosis of GJ in form of annular GJs [Watanabe et al, 1988].…”

Section: Gap Junction Removal and Degradationmentioning

confidence: 88%

“…Consistent with these data were further electron microscopical studies characterizing the plasma membrane and its cytoskeletal undercoat at sites of GJ invagination. Here, invaginating GJs revealed a network of actin-containing microfilaments [Watanabe et al, 1988]. In deeper invaginations of withdrawing GJs, parallel microfilament arrays formed a submembraneous sheath with an orthogonal arrangement toward the long axis of the invagination.…”

Section: Gap Junction Removal and Degradationmentioning

confidence: 94%

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Connexins, cell motility, and the cytoskeleton

Olk

Zoidl

Dermietzel

2009

Cell Motil. Cytoskeleton

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Connexins (Cx) comprise a family of transmembrane proteins, which form intercellular channels between plasma membranes of two adjoining cells, commonly known as gap junctions. Recent reports revealed that Cx proteins interact with diverse cellular components to form a multiprotein complex, which has been termed “Nexus”. Potential interaction partners include proteins such as cytoskeletal proteins, scaffolding proteins, protein kinases and phosphatases. These interactions allow correct subcellular localization of Cxs and functional regulation of gap junction‐mediated intercellular communication. Evidence is accruing that Cxs might have channel‐independent functions, which potentially include regulation of cell migration, cell polarization and growth control. In the current review, we summarize recent knowledge on Cx interactions with cytoskeletal proteins and highlight some aspects of their role in cellular motility. Cell Motil. Cytoskeleton 66: 1000–1016, 2009. © 2009 Wiley‐Liss, Inc.

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Section: Gap Junction Removal and Degradationmentioning

confidence: 88%

Section: Gap Junction Removal and Degradationmentioning

confidence: 94%

Connexins, cell motility, and the cytoskeleton

Olk

Zoidl

Dermietzel

2009

Cell Motil. Cytoskeleton

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“…By freeze-etching with a cryoprotectant (methanol) [17,18], we can get around the many difficulties involved in other methods as described previously [19]. Lectin labeling combined with this method proves beneficial in giving a two-dimensional overview of labeling particles as well as the examination of lectin-induced secondary changes of the glycoconjugate distribution on the luminal surface of the rod outer segment disk membrane.…”

Section: Discussionmentioning

confidence: 99%

Investigation of Luminal Surface Structures of Rod Photoreceptor Outer Segments by Lectin Cytochemistry Combined with Freeze-Etching

et al. 1999

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The luminal surface of the rod photoreceptor disk membrane was exposed by means of osmotic shock and labeled with ferritin- conjugated concanavalin A. The structural changes of the luminal surface were examined by a freeze-etching procedure with cryoprotectant (methanol). On replicas from freeze-etched membranes with concanavalin A labeling, 6- to 10-nm particles were codistributed with ferritin particles on the luminal surface of the disk membrane. By contrast, there were few ferritin particles or less numerous 6- to 10-nm particles on the corresponding surface without concanavalin A labeling. If 6- to 10-nm particles corresponded to the carbohydrate moiety of rhodopsin, concanavalin A binding might tend to preserve this carbohydrate moiety. These results suggest that the two-dimensional analysis of lectin-induced structural changes of the membrane surface glycoconjugates may become available by lectin cytochemistry combined with freeze-etching.

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“…How the junctions are anchored is not yet clear. It has been claimed a number of times that gap junctions interact with cytoskeletal elements (3,9), although this is not universally accepted (5) . The well anchored plaques may be located in regions where the lipid has not been completely removed, or be plaques that have strong connections to cytoskeletal or other cellular structures, either naturally or as a result of fixation.…”

Section: And Discussionmentioning

confidence: 99%