Interaction of microtubules and actin with the N-terminus of beta Pix-b(L) directs cellular pinocytosis
DC Field | Value | Language |
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dc.contributor.author | Lee, Seung Joon | - |
dc.contributor.author | Yang, Soo Jung | - |
dc.contributor.author | Kim, Dae Hwan | - |
dc.contributor.author | Pak, Jhang Ho | - |
dc.contributor.author | Lee, Kwang Ho | - |
dc.contributor.author | Choi, Kyoung Hee | - |
dc.contributor.author | Park, Dongeun | - |
dc.contributor.author | Rhee, Sangmyung | - |
dc.date.available | 2019-05-29T13:34:43Z | - |
dc.date.issued | 2011-05 | - |
dc.identifier.issn | 0300-8177 | - |
dc.identifier.issn | 1573-4919 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/21549 | - |
dc.description.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. | - |
dc.format.extent | 9 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | SPRINGER | - |
dc.title | Interaction of microtubules and actin with the N-terminus of beta Pix-b(L) directs cellular pinocytosis | - |
dc.type | Article | - |
dc.identifier.doi | 10.1007/s11010-011-0728-2 | - |
dc.identifier.bibliographicCitation | MOLECULAR AND CELLULAR BIOCHEMISTRY, v.351, no.1-2, pp 207 - 215 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000288963800023 | - |
dc.identifier.scopusid | 2-s2.0-79953699329 | - |
dc.citation.endPage | 215 | - |
dc.citation.number | 1-2 | - |
dc.citation.startPage | 207 | - |
dc.citation.title | MOLECULAR AND CELLULAR BIOCHEMISTRY | - |
dc.citation.volume | 351 | - |
dc.type.docType | Article | - |
dc.publisher.location | 네델란드 | - |
dc.subject.keywordAuthor | beta Pix | - |
dc.subject.keywordAuthor | Pinocytosis | - |
dc.subject.keywordAuthor | Calponin homology domain | - |
dc.subject.keywordAuthor | Actin | - |
dc.subject.keywordAuthor | Microtubule | - |
dc.subject.keywordAuthor | Cell spreading | - |
dc.subject.keywordPlus | CALPONIN HOMOLOGY DOMAIN | - |
dc.subject.keywordPlus | LAMELLIPODIA FORMATION | - |
dc.subject.keywordPlus | MEMBRANE RUFFLES | - |
dc.subject.keywordPlus | EXCHANGE FACTOR | - |
dc.subject.keywordPlus | FOCAL ADHESION | - |
dc.subject.keywordPlus | BETA-PIX | - |
dc.subject.keywordPlus | MACROPINOCYTOSIS | - |
dc.subject.keywordPlus | LOCALIZATION | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | P21-ACTIVATED-KINASE-1 | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.description.journalRegisteredClass | sci | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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