scholarly journals Phospholipase Cζ (PLCζ) versus postacrosomal sheath WW domain‐binding protein (PAWP): Which molecule will survive as a sperm factor?

2020 ◽  
Vol 91 (1) ◽  
Author(s):  
Michiko Nakai ◽  
Junya Ito ◽  
Ayumi Suyama ◽  
Atsuko Kageyama ◽  
Yasuko Tobari ◽  
...  
Keyword(s):  
Binding Protein ◽  
Ww Domain ◽  
Sperm Factor

Sperm‐derived WW domain‐binding protein, PAWP, elicits calcium oscillations and oocyte activation in humans and mice

2014 ◽  
Vol 28 (10) ◽  
pp. 4434-4440 ◽  
Author(s):  
Mahmoud Aarabi ◽  
Hanna Balakier ◽  
Siamak Bashar ◽  
Sergey I. Moskovtsev ◽  
Peter Sutovsky ◽  
...  
Keyword(s):  
Binding Protein ◽  
Calcium Oscillations ◽  
Oocyte Activation ◽  
Ww Domain

scholarly journals WW domain-binding protein 2: an adaptor protein closely linked to the development of breast cancer

2017 ◽  
Vol 16 (1) ◽  
Author(s):  
Shuai Chen ◽  
Han Wang ◽  
Yu-Fan Huang ◽  
Ming-Li Li ◽  
Jiang-Hong Cheng ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Binding Protein ◽  
Adaptor Protein ◽  
Ww Domain

scholarly journals PAWP, a Sperm-specific WW Domain-binding Protein, Promotes Meiotic Resumption and Pronuclear Development during Fertilization

2007 ◽  
Vol 282 (16) ◽  
pp. 12164-12175 ◽  
Author(s):  
Alexander T. H. Wu ◽  
Peter Sutovsky ◽  
Gaurishankar Manandhar ◽  
Wei Xu ◽  
Mika Katayama ◽  
...  
Keyword(s):  
Binding Protein ◽  
Ww Domain

scholarly journals WBP-2, a WW domain binding protein, interacts with the thyroid-specific transcription factor Pax8

2004 ◽  
Vol 377 (3) ◽  
pp. 553-560 ◽  
Author(s):  
Roberto NITSCH ◽  
Tina DI PALMA ◽  
Anna MASCIA ◽  
Mariastella ZANNINI
Keyword(s):  
Protein Interaction ◽  
Transcriptional Activation ◽  
Binding Protein ◽  
Interaction Domain ◽  
Ww Domain ◽  
Transcriptional Activation Domain ◽  
Culture Cells ◽  
C Terminus

The Pax gene family encodes transcription factors that are essential in organogenesis and in the differentiation of various organs in higher eukaryotes. Pax proteins have a DNA binding domain at the N-terminus, and a transcriptional activation domain at the C-terminus. How these domains interact with the transcriptional machinery of the cell is still unclear. In the present paper, we describe the identification by means of immunological screening of the WW domain binding protein WBP-2 as a biochemical interactor of Pax8 (a WW domain is a protein-interaction domain containing two conserved tryptophan residues). Pax8 is required for the morphogenesis of the thyroid gland and for the maintenance of the thyroid differentiated cellular phenotype. WBP-2 was identified originally as a WW domain binding protein, and its function is still unknown. WBP-2 binds to Pax8 in vitro in pulldown assays, and in vivo in tissue culture cells in co-immunoprecipitation assays. Interestingly, Pax8 does not contain a WW domain. Our results point to the identification of a new protein-interacting domain that is present in the C-terminal portion of Pax8 and that is required for protein–protein interaction with WBP-2. Our results demonstrate that WBP-2 is not a transcriptional co-activator of Pax8, but rather behaves as an adaptor molecule, as suggested in other studies.

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