A Golgi-associated protein 4.1B variant is required for assimilation of proteins in the membrane

Kang, Qiaozhen; Wang, Ting; Zhang, Huizheng; Mohandas, Narla; An, Xiuli

doi:10.1242/jcs.039644

Cited by 31 publications

(32 citation statements)

References 35 publications

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“…The whole-cell lysates of CD4 ϩ T cells or thymocytes (10 6 cells) were separated by 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to polyvinylidene difluoride (PVDF) membrane (Millipore, Billerica, MA). The membrane was probed with antibodies against 4.1R exon 13, 4.1B headpiece, 4.1G headpiece, and 4.1N headpiece, 32 followed by horseradish peroxidase (HRP)-conjugated goat anti-rabbit IgG (Jackson ImmunoResearch Laboratories, West Grove, PA). The film was developed with the use of the Renaissance chemiluminescence detection kit (Pierce, Rockford, IL).…”

Section: Immunoblot Analysismentioning

confidence: 99%

“…24,32 Lobe A, lobe B, and lobe C of the 30-kDa membrane binding domain were subcloned into pGEX-4T-2 vector (GE Healthcare, Little Chalfont, United Kingdom) with EcoRI and SalI upstream and downstream, respectively. The cytoplasmic domain of LAT was cloned into pMAL-p2x vector (New England BioLabs) with BamHI and SalI or into pET28b(ϩ) vector (Novagen, Madison, WI) with the use of NcoI and NotI upstream and downstream, respectively.…”

Section: Construction Expression and Purification Of Recombinant 4mentioning

confidence: 99%

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Cytoskeletal protein 4.1R negatively regulates T-cell activation by inhibiting the phosphorylation of LAT

Kang¹,

Yu²,

Pei³

et al. 2009

Blood

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Section: Immunoblot Analysismentioning

confidence: 99%

Section: Construction Expression and Purification Of Recombinant 4mentioning

confidence: 99%

Cytoskeletal protein 4.1R negatively regulates T-cell activation by inhibiting the phosphorylation of LAT

Kang¹,

Yu²,

Pei³

et al. 2009

Blood

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“…These include the nucleus (6), nuclear matrix (7), centrosome (8), and immunological synapse (9). In particular, it has been shown that 4.1R is expressed in many epithelial tissues (10,11) and epithelial cell lines (12,13). However, the function of 4.1R in these cells, particularly the function of 4.1R in vivo, remains largely unexplored.…”

mentioning

confidence: 99%

Impaired Intestinal Calcium Absorption in Protein 4.1R-deficient Mice Due to Altered Expression of Plasma Membrane Calcium ATPase 1b (PMCA1b)

Liu

Weng

Chen

et al. 2013

Journal of Biological Chemistry

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Background:The function of protein 4.1R in small intestinal epithelia is unknown. Results: 4.1R deficiency resulted in decreased expression of PMCA1b and impaired small intestinal calcium absorption. Conclusion: Protein 4.1R plays an important role in small intestinal calcium absorption. Significance: Our results identify a novel function for protein 4.1R and offer new insights into the mechanism of calcium absorption.

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“…47,48 induce AJ disassembly in follicle epithelium, 39 whereas depletion of mammalian βII-spectrin attenuated formation of AJs in human intestinal and bronchial epithelial cells, 32,40 and early mouse embryo. 41 Two major mechanisms can be responsible for the observed spectrin-dependent regulation of epithelial junctions.…”

Section: Adducin Regulates Remodeling Of Apical Junctions In Simple Ementioning

confidence: 97%

Spectrin-adducin membrane skeleton

Naydenov

Ivanov

2011

BioArchitecture

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PersPective 186BioArchitecture volume 1 issue 4 Such junctional plasticity depends on the orchestrated dynamics of the plasma membrane with its underlying F-actin cytoskeleton, however the interplay between these cellular structures remains poorly understood. Recent studies highlighted the spectrin-adducin-based membrane skeleton as an emerging regulator of AJ and TJ integrity and remodeling. Here we discuss new evidences implicating adducin, spectrin and other membrane skeleton proteins in stabilization of epithelial junctions and regulation of junctional dynamics. Based on the known ability of the membrane skeleton to link cortical actin filaments to the plasma membrane, we hypothesize that the spectrin-adducin network serves as a critical signal and force transducer from the actomyosin cytoskeleton to junctions during remodeling of AJs and TJs. IntroductionIntegrity and barrier properties of epithelial layers depend on the assembly of adhesive contacts between adjacent epithelial cells. These adhesive contacts are composed of multiprotein complexes known as intercellular junctions. In simple polarized epithelia, several junctional complexes span the lateral plasma membrane to interact with opposing complementary Spectrin-adducin membrane skeletonA missing link between epithelial junctions and the actin cytoskeletion? Nayden G. Naydenov and Andrei I. Ivanov* Department of Medicine; University of Rochester; Rochester, NY USA junctions in the intercellular space and associate with various cytoskeletal, signaling and trafficking components at the cytosolic face of the membrane.1,2 Among these complexes the most apically-located tight junctions (TJs) and subjacent adherens junctions (AJs) play key roles in regulating epithelial cell adhesion, polarity and differentiation. [2][3][4][5] TJs and AJs are composed of several types of integral membrane and cytosolic scaffolding proteins. Major transmembrane components of TJs mediating intercellular adhesions include the claudin protein family, occludin and junctional adhesion molecule A.2,3,5 'Zonula occludens' (ZO) proteins are the most abundant molecular constituents of the cytosolic plaque of TJs. 2,3,5,6 Adhesive properties of epithelial AJs are determined by E-cadherin and nectins, which are clustered and stabilized at the plasma membrane via interactions with cytosolic scaffolds such as α, β and p120 catenins. 2,4,7 Once considered as static, glue-like structures, TJs and AJs are now known to be very dynamic. Such dynamics includes a continuous remodeling (disassembly and reassembly) of junctional complexes in fully-differentiated epithelial layers, as well as large-scale TJ/AJ rearrangements that occur during normal epithelial morphogenesis and disruption of mucosal barriers in many diseases. [8][9][10][11][12] Two major mechanisms have been implicated in regulation of junctional dynamics; one is reorganizations of the perijunctional F-actin cytoskeleton and the other is remodeling of the plasma membrane. [8][9][10][11][12][13] The interplay between these mechani...

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A Golgi-associated protein 4.1B variant is required for assimilation of proteins in the membrane

Cited by 31 publications

References 35 publications

Cytoskeletal protein 4.1R negatively regulates T-cell activation by inhibiting the phosphorylation of LAT

Cytoskeletal protein 4.1R negatively regulates T-cell activation by inhibiting the phosphorylation of LAT

Impaired Intestinal Calcium Absorption in Protein 4.1R-deficient Mice Due to Altered Expression of Plasma Membrane Calcium ATPase 1b (PMCA1b)

Spectrin-adducin membrane skeleton

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