scholarly journals Correction: A Golgi-associated protein 4.1B variant is required for assimilation of proteins in the membrane (doi:10.1242/jcs.039644)

2019 ◽  
Vol 132 (20) ◽  
pp. jcs240002
Author(s):  
Qiaozhen Kang ◽  
Ting Wang ◽  
Huizheng Zhang ◽  
Narla Mohandas ◽  
Xiuli An
Keyword(s):  
Protein 4.1B

scholarly journals SynCAM1 recruits NMDA receptors via Protein 4.1B

2009 ◽  
Vol 42 (4) ◽  
pp. 466-483 ◽  
Author(s):  
Jennifer L. Hoy ◽  
John R. Constable ◽  
Stefano Vicini ◽  
Zhanyan Fu ◽  
Philip Washbourne
Keyword(s):  
Nmda Receptors ◽  
Protein 4.1B

scholarly journals Molecular and Functional Characterization of Protein 4.1B, a Novel Member of the Protein 4.1 Family with High Level, Focal Expression in Brain

2000 ◽  
Vol 275 (5) ◽  
pp. 3247-3255 ◽  
Author(s):  
Marilyn Parra ◽  
Philippe Gascard ◽  
Loren D. Walensky ◽  
J. Aura Gimm ◽  
Seth Blackshaw ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Protein 4.1 ◽  
High Level ◽  
Focal Expression ◽  
Protein 4.1B

scholarly journals Pivotal roles of protein 4.1B/DAL‑1, a FERM‑domain containing protein, in tumor progression (Review)

2019 ◽  
Author(s):  
Xiaofeng Yuan ◽  
Lianhua Piao ◽  
Luhui Wang ◽  
Xu Han ◽  
Ming Zhuang ◽  
...  
Keyword(s):  
Tumor Progression ◽  
Ferm Domain ◽  
Protein 4.1B

Immunolocalization of protein 4.1B/DAL-1 during neoplastic transformation of mouse and human intestinal epithelium

2004 ◽  
Vol 122 (6) ◽  
pp. 579-586 ◽  
Author(s):  
Nobuhiko Ohno ◽  
Nobuo Terada ◽  
Shin-ichi Murata ◽  
Hisashi Yamakawa ◽  
Irene F. Newsham ◽  
...  
Keyword(s):  
Intestinal Epithelium ◽  
Neoplastic Transformation ◽  
Human Intestinal Epithelium ◽  
Protein 4.1B

Tumor suppressor role of protein 4.1B/DAL-1

2014 ◽  
Vol 71 (24) ◽  
pp. 4815-4830 ◽  
Author(s):  
Zi Wang ◽  
Ji Zhang ◽  
Mao Ye ◽  
Min Zhu ◽  
Bin Zhang ◽  
...  
Keyword(s):  
Tumor Suppressor ◽  
Protein 4.1B

Protein 4.1B localizes on unmyelinated axonal membranes in the mouse enteric nervous system

2004 ◽  
Vol 366 (1) ◽  
pp. 15-17 ◽  
Author(s):  
Nobuo Terada ◽  
Nobuhiko Ohno ◽  
Hisashi Yamakawa ◽  
Takeshi Baba ◽  
Yasuhisa Fujii ◽  
...  
Keyword(s):  
Nervous System ◽  
Enteric Nervous System ◽  
Protein 4.1B

scholarly journals Protein 4.1B Suppresses Tumor Metastasis by Regulating Epithelial-mesenchymal Transition Progression in Melanoma Cells

2019 ◽  
Vol 16 (4) ◽  
pp. 529-536 ◽  
Author(s):  
Chengbo Wang ◽  
Keyan Li ◽  
Yingli Men ◽  
Cong Ding ◽  
Juan Du ◽  
...  
Keyword(s):  
Tumor Metastasis ◽  
Epithelial Mesenchymal Transition ◽  
Melanoma Cells ◽  
Mesenchymal Transition ◽  
Protein 4.1B

scholarly journals Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr

2002 ◽  
Vol 157 (7) ◽  
pp. 1247-1256 ◽  
Author(s):  
Leora Gollan ◽  
Helena Sabanay ◽  
Sebastian Poliak ◽  
Erik O. Berglund ◽  
Barbara Ranscht ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Adhesion Molecules ◽  
Cytoplasmic Domain ◽  
Short Sequence ◽  
Extracellular Region ◽  
A Cell ◽  
Adhesion Complex ◽  
Protein 4.1B

An axonal complex of cell adhesion molecules consisting of Caspr and contactin has been found to be essential for the generation of the paranodal axo-glial junctions flanking the nodes of Ranvier. Here we report that although the extracellular region of Caspr was sufficient for directing it to the paranodes in transgenic mice, retention of the Caspr–contactin complex at the junction depended on the presence of an intact cytoplasmic domain of Caspr. Using immunoelectron microscopy, we found that a Caspr mutant lacking its intracellular domain was often found within the axon instead of the junctional axolemma. We further show that a short sequence in the cytoplasmic domain of Caspr mediated its binding to the cytoskeleton-associated protein 4.1B. Clustering of contactin on the cell surface induced coclustering of Caspr and immobilized protein 4.1B at the plasma membrane. Furthermore, deletion of the protein 4.1B binding site accelerated the internalization of a Caspr–contactin chimera from the cell surface. These results suggest that Caspr serves as a “transmembrane scaffold” that stabilizes the Caspr/contactin adhesion complex at the paranodal junction by connecting it to cytoskeletal components within the axon.

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