Article: [Advances in the study of the actin nucleation factor Spire].
Sheng li xue bao : [Acta physiologica Sinica
2024 Volume 76, Issue 2, Page(s) 341–345
Abstract: There are three main classes of actin nucleation factors: Arp2/3 complexes, Spire and Formin. Spire assembles microfilaments by nucleating stable longitudinal tetramers and binding actin to the growing end of the microfilament. As early as 1999, ... ...
Abstract | There are three main classes of actin nucleation factors: Arp2/3 complexes, Spire and Formin. Spire assembles microfilaments by nucleating stable longitudinal tetramers and binding actin to the growing end of the microfilament. As early as 1999, Wellington et al. identified Spire as an actin nucleating agent, however, over the years, most studies have focused on Arp2/3 and Formin proteins; there has been relatively less research on Spire as a member of the actin nucleating factors. Recent studies have shown that Spire is involved in the vesicular transport through the synthesis of actin and plays an important role in neural development. In this paper, we reviewed the structure, expression and function of Spire, and its association with disease in order to identify meaningful potential directions for studies on Spire. |
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MeSH term(s) | Microfilament Proteins/metabolism ; Microfilament Proteins/physiology ; Humans ; Animals ; Actins/metabolism ; Actins/physiology ; Actin-Related Protein 2-3 Complex/metabolism ; Actin Cytoskeleton/metabolism ; Actin Cytoskeleton/physiology ; Nuclear Proteins |
Chemical Substances | Microfilament Proteins ; Actins ; Actin-Related Protein 2-3 Complex ; SPIRE1 protein, human ; Nuclear Proteins |
Language | Chinese |
Publishing date | 2024-04-24 |
Publishing country | China |
Document type | Journal Article ; Review ; Research Support, Non-U.S. Gov't ; English Abstract |
ZDB-ID | 604308-2 |
ISSN | 0371-0874 |
ISSN | 0371-0874 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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