Direct Interaction between the Intracellular Domains of Bullous Pemphigoid Antigen 2 (BP180) and β4 Integrin, Hemidesmosomal Components of Basal Keratinocytes

1998 ◽  
Vol 243 (3) ◽  
pp. 694-699 ◽  
Author(s):  
Sirpa Aho ◽  
Jouni Uitto
Keyword(s):  
Bullous Pemphigoid ◽  
Direct Interaction ◽  
Basal Keratinocytes ◽  
Bullous Pemphigoid Antigen ◽  
Intracellular Domains ◽  
Β4 Integrin

scholarly journals Hemidesmosome Formation Is Initiated by the β4 Integrin Subunit, Requires Complex Formation of β4 and HD1/Plectin, and Involves a Direct Interaction between β4 and the Bullous Pemphigoid Antigen 180

1998 ◽  
Vol 142 (1) ◽  
pp. 271-284 ◽  
Author(s):  
Roel Q.J. Schaapveld ◽  
Luca Borradori ◽  
Dirk Geerts ◽  
Manuel R. van Leusden ◽  
Ingrid Kuikman ◽  
...  
Keyword(s):  
Bullous Pemphigoid ◽  
Direct Interaction ◽  
Cytoplasmic Domain ◽  
Integrin Subunit ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Fibronectin Type Iii ◽  
Activation Motif ◽  
Β4 Integrin ◽  
Two Hybrid

Hemidesmosomes (HDs) are stable anchoring structures that mediate the link between the intermediate filament cytoskeleton and the cell substratum. We investigated the contribution of various segments of the β4 integrin cytoplasmic domain in the formation of HDs in transient transfection studies using immortalized keratinocytes derived from an epidermolysis bullosa patient deficient in β4 expression. We found that the expression of wild-type β4 restored the ability of the β4-deficient cells to form HDs and that distinct domains in the NH2- and COOH-terminal regions of the β4 cytoplasmic domain are required for the localization of HD1/plectin and the bullous pemphigoid antigens 180 (BP180) and 230 (BP230) in these HDs. The tyrosine activation motif located in the connecting segment (CS) of the β4 cytoplasmic domain was dispensable for HD formation, although it may be involved in the efficient localization of BP180. Using the yeast two-hybrid system, we could demonstrate a direct interaction between β4 and BP180 which involves sequences within the COOH-terminal part of the CS and the third fibronectin type III (FNIII) repeat. Immunoprecipitation studies using COS-7 cells transfected with cDNAs for α6 and β4 and a mutant BP180 which lacks the collagenous extracellular domain confirmed the interaction of β4 with BP180. Nevertheless, β4 mutants which contained the BP180-binding region, but lacked sequences required for the localization of HD1/plectin, failed to localize BP180 in HDs. Additional yeast two- hybrid assays indicated that the 85 COOH-terminal residues of β4 can interact with the first NH2-terminal pair of FNIII repeats and the CS, suggesting that the cytoplasmic domain of β4 is folded back upon itself. Unfolding of the cytoplasmic domain may be part of a mechanism by which the interaction of β4 with other hemidesmosomal components, e.g., BP180, is regulated.

scholarly journals BPAG1e Maintains Keratinocyte Polarity through β4 Integrin–mediated Modulation of Rac 1 and Cofilin Activities

2009 ◽  
Vol 20 (12) ◽  
pp. 2954-2962 ◽  
Author(s):  
Kevin J. Hamill ◽  
Susan B. Hopkinson ◽  
Philip DeBiase ◽  
Jonathan C.R. Jones
Keyword(s):  
Signal Transduction ◽  
Cell Surface ◽  
Bullous Pemphigoid ◽  
Wild Type ◽  
Expression Levels ◽  
Bullous Pemphigoid Antigen ◽  
Affect Expression ◽  
Α6β4 Integrin ◽  
And Migration ◽  
Β4 Integrin

α6β4 integrin, a component of hemidesmosomes, also plays a role in keratinocyte migration via signaling through Rac1 to the actin-severing protein cofilin. Here, we tested the hypothesis that the β4 integrin-associated plakin protein, bullous pemphigoid antigen 1e (BPAG1e) functions as a scaffold for Rac1/cofilin signal transduction. We generated keratinocyte lines exhibiting a stable knockdown in BPAG1e expression. Knockdown of BPAG1e does not affect expression levels of other hemidesmosomal proteins, nor the amount of β4 integrin expressed at the cell surface. However, the amount of Rac1 associating with β4 integrin and the activity of both Rac1 and cofilin are significantly lower in BPAG1e-deficient cells compared with wild-type keratinocytes. In addition, keratinocytes deficient in BPAG1e exhibit loss of front-to-rear polarity and display aberrant motility. These defects are rescued by inducing expression of constitutively active Rac1 or active cofilin. These data indicate that the BPAG1e is required for efficient regulation of keratinocyte polarity and migration by determining the activation of Rac1.

Activation of bullous pemphigoid antigen gene in mouse ear epidermis by ultraviolet radiation

1998 ◽  
Vol 16 ◽  
pp. S228
Author(s):  
Ken-ichi Kayashima ◽  
Takehiko Koji ◽  
Masayuki Nozawa ◽  
Tomomichi Ono ◽  
Paul K. Nakane
Keyword(s):  
Ultraviolet Radiation ◽  
Bullous Pemphigoid ◽  
Antigen Gene ◽  
Bullous Pemphigoid Antigen ◽  
Mouse Ear

A 230-kD Basic Protein Is the Major Bullous Pemphigoid Antigen

1989 ◽  
Vol 92 (1) ◽  
pp. 33-38 ◽  
Author(s):  
Stephan Mueller ◽  
Vera Klaus-Kovtun ◽  
John R. Stanley
Keyword(s):  
Bullous Pemphigoid ◽  
Basic Protein ◽  
Bullous Pemphigoid Antigen

Pemphigoid Nodularis: A Case with 230 kDa Hemidesmosomes Antigen Associated with Bullous Pemphigoid Antigen

1995 ◽  
Vol 22 (3) ◽  
pp. 201-204 ◽  
Author(s):  
Yasuhiko Tamada ◽  
Kikuka Yokochi ◽  
Yoshimi Oshitani ◽  
Yukiko Nitta ◽  
Toshihiko Ikeya ◽  
...  
Keyword(s):  
Bullous Pemphigoid ◽  
Bullous Pemphigoid Antigen ◽  
Pemphigoid Nodularis
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