Interaction of microtubules and actin with the N-terminus of beta Pix-b(L) directs cellular pinocytosis
- Authors
- Lee, Seung Joon; Yang, Soo Jung; Kim, Dae Hwan; Pak, Jhang Ho; Lee, Kwang Ho; Choi, Kyoung Hee; Park, Dongeun; Rhee, Sangmyung
- Issue Date
- May-2011
- Publisher
- SPRINGER
- Keywords
- beta Pix; Pinocytosis; Calponin homology domain; Actin; Microtubule; Cell spreading
- Citation
- MOLECULAR AND CELLULAR BIOCHEMISTRY, v.351, no.1-2, pp 207 - 215
- Pages
- 9
- Journal Title
- MOLECULAR AND CELLULAR BIOCHEMISTRY
- Volume
- 351
- Number
- 1-2
- Start Page
- 207
- End Page
- 215
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/21549
- DOI
- 10.1007/s11010-011-0728-2
- ISSN
- 0300-8177
1573-4919
- Abstract
- beta Pix is a Rac/Cdc42 guanine nucleotide exchange factor (GEF) that is known to be a regulator of actin cytoskeleton remodeling. Recently, a novel splicing isoform, beta Pix-b(L), was identified as an alternative translational product of the beta Pix-b mRNA with an extended N-terminus comprising a partial calponin homology (CH) domain and a serine-rich (SR) domain. However, the cellular function of beta Pix-b(L) is largely unknown. In the current study, we analyzed the genomic DNA structure and cellular functions of beta Pix-b(L). The results of this study demonstrate that beta Pix is composed of 24 exons and 21 introns spanning around 100 kb. RT-PCR experiments revealed that there are two forms of beta Pix mRNA with distinct 5' UTRs that are the result of alternative splicing of exon 1 and 2 from beta Pix genomic DNA. In addition, affinity chromatography analysis and a pull-down assay with the N-terminal region of beta Pix-b(L) revealed that beta Pix-b(L) interacts with tubulin and actin via its N-terminal CH and SR domains, respectively. Interaction with tubulin enabled beta Pix-b(L) to bundle the microtubule and form membrane protrusions. Furthermore, the N-terminus of beta Pix-b(L) was also critical for its localization to cellular vesicles. Functionally, beta Pix-b(L) induced pinocytosis through cooperative action of the CH and Dbl homology (DH) domains, demonstrating the role of beta Pix-b(L) in the regulation of membrane dynamics.
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Collections - College of Natural Sciences > Department of Life Science > 1. Journal Articles
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