Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/05/15 23:10:14」(JST)

wiki en

Gelsolin is an actin-binding protein that is a key regulator of actin filament assembly and disassembly. Gelsolin is one of the most potent members of the actin-severing gelsolin/villin superfamily, as it severs with nearly 100% efficiency.^[1]^[2] Gelsolin is located intracellularly (in cytosol and mitochondria) and extracellularly (in blood plasma).^[3]

Structure

Gelsolin is an 82-kD protein with six homologous subdomains, referred to as S1-S6. Each subdomain is composed of a five-stranded β-sheet, flanked by two α-helices, one positioned perpendicular with respect to the strands and one positioned parallel. The N-terminal (S1-S3) forms an extended β-sheet, as does the C-terminal (S4-S6).^[4]

Regulation

Among the lipid-binding actin regulatory proteins, gelsolin (along with cofilin) is one of the few that exhibit preferential binding toward polyphosphoinositide (PPIs).^[5] The binding sequences in gelsolin closely resemble the motifs in the other PPI-binding proteins.^[5]

Gelsolin's activity is stimulated by calcium ions (Ca²⁺).^[2] Although the protein retains its overall structural integrity in both activated and deactivated states, the S6 helical tail moves like a latch depending on the concentration of calcium ions.^[6] The C-terminal end detects the calcium concentration within the cell. When there is no Ca²⁺ present, the tail of S6 shields the actin-binding sites on one of S2's helices.^[4] When a calcium ion attaches to the S6 tail, however, it straightens, exposing the S2 actin-binding sites.^[6] The N-terminal is directly involved in the severing of actin. S2 and S3 bind to the actin before the binding of S1 severs actin-actin bonds and caps the barbed end.^[5]

Gelsolin can be inhibited by a local rise in the concentration of phosphatidylinositol (4,5)-bisphosphate (PIP₂), a PPI. This is a two step process. Firstly, (PIP₂) binds to S2 and S3, inhibiting gelsolin from actin side binding. Then, (PIP₂) binds to gelsolin’s S1, preventing gelsolin from severing actin, although (PIP₂) does not bind directly to gelsolin's actin-binding site.^[5]

Gelsolin's severing of actin, in contrast to the severing of microtubules by katanin, does not require any extra energy input.

Cellular function

As an important actin regulator, gelsolin plays a role in podosome formation (along with Arp3, cortactin, and Rho GTPases).^[7]

Gelsolin also inhibits apoptosis by stabilizing the mitochondria.^[3] Prior to cell death, mitochondria normally lose membrane potential and become more permeable. Gelsolin can impede the release of cytochrome C, obstructing the signal amplification that would have led to apoptosis.^[8]

Actin can be cross-linked into a gel by actin cross-linking proteins. Gelsolin can turn this gel into a sol, hence the name gelsolin.

Animal studies

Research in mice suggests that gelsolin, like other actin-severing proteins, is not expressed to a significant degree until after the early embryonic stage—approximately 2 weeks in murine embryos.^[9] In adult specimens, however, gelsolin is particularly important in motile cells, such as blood platelets. Mice with null gelsolin-coding genes undergo normal embryonic development, but the deformation of their blood platelets reduced their motility, resulting in a slower response to wound healing.^[9]

An insufficiency of gelsolin in mice has also been shown to cause increased permeability of the vascular pulmonary barrier, suggesting that gelsolin is important in the response to lung injury.^[10]

Related proteins

Sequence comparisons indicate an evolutionary relationship between gelsolin, villin, fragmin and severin.^[11] Six large repeating segments occur in gelsolin and villin, and 3 similar segments in severin and fragmin. While the multiple repeats have yet to be related to any known function of the actin-severing proteins, the superfamily appears to have evolved from an ancestral sequence of 120 to 130 amino acid residues.^[1]^[11]

Interactions

Gelsolin is a cytoplasmic, calcium-regulated, actin-modulating protein that binds to the barbed ends of actin filaments, preventing monomer exchange (end-blocking or capping).^[12] It can promote nucleation (the assembly of monomers into filaments), as well as sever existing filaments. In addition, this protein binds with high affinity to fibronectin. Plasma gelsolin and cytoplasmic gelsolin are derived from a single gene by alternate initiation sites and differential splicing.

Gelsolin has been shown to interact with:

Amyloid precursor protein,^[13]
Androgen receptor,^[14]
PTK2B,^[15] and
VDAC1.^[8]

References

^ ^a ^b Ghoshdastider U, Popp D, Burtnick LD, Robinson RC (2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton (Hoboken) 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256.
^ ^a ^b Sun HQ, Yamamoto M, Mejillano M, Yin HL (November 1999). "Gelsolin, a multifunctional actin regulatory protein". J. Biol. Chem. 274 (47): 33179–82. doi:10.1074/jbc.274.47.33179. PMID 10559185.
^ ^a ^b Koya RC, Fujita H, Shimizu S, Ohtsu M, Takimoto M, Tsujimoto Y, Kuzumaki N (May 2000). "Gelsolin inhibits apoptosis by blocking mitochondrial membrane potential loss and cytochrome c release". J. Biol. Chem. 275 (20): 15343–9. doi:10.1074/jbc.275.20.15343. PMID 10809769.
^ ^a ^b Kiselar JG, Janmey PA, Almo SC, Chance MR (April 2003). "Visualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprinting". Proc. Natl. Acad. Sci. U.S.A. 100 (7): 3942–7. doi:10.1073/pnas.0736004100. PMC 153027. PMID 12655044.
^ ^a ^b ^c ^d Yu FX, Sun HQ, Janmey PA, Yin HL (July 1992). "Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin". J. Biol. Chem. 267 (21): 14616–21. PMID 1321812.
^ ^a ^b Burtnick LD, Urosev D, Irobi E, Narayan K, Robinson RC (July 2004). "Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF". EMBO J. 23 (14): 2713–22. doi:10.1038/sj.emboj.7600280. PMC 514944. PMID 15215896.
^ Varon C, Tatin F, Moreau V, Van Obberghen-Schilling E, Fernandez-Sauze S, Reuzeau E, Kramer I, Génot E (May 2006). "Transforming growth factor beta induces rosettes of podosomes in primary aortic endothelial cells". Mol. Cell. Biol. 26 (9): 3582–94. doi:10.1128/MCB.26.9.3582-3594.2006. PMC 1447430. PMID 16611998.
^ ^a ^b Kusano H, Shimizu S, Koya RC, Fujita H, Kamada S, Kuzumaki N, Tsujimoto Y (October 2000). "Human gelsolin prevents apoptosis by inhibiting apoptotic mitochondrial changes via closing VDAC". Oncogene 19 (42): 4807–14. doi:10.1038/sj.onc.1203868. PMID 11039896.
^ ^a ^b Witke W, Sharpe AH, Hartwig JH, Azuma T, Stossel TP, Kwiatkowski DJ (April 1995). "Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin". Cell 81 (1): 41–51. doi:10.1016/0092-8674(95)90369-0. PMID 7720072.
^ Becker PM, Kazi AA, Wadgaonkar R, Pearse DB, Kwiatkowski D, Garcia JG (April 2003). "Pulmonary vascular permeability and ischemic injury in gelsolin-deficient mice". Am. J. Respir. Cell Mol. Biol. 28 (4): 478–84. doi:10.1165/rcmb.2002-0024OC. PMID 12654637.
^ ^a ^b Way M, Weeds A (October 1988). "Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats". J. Mol. Biol. 203 (4): 1127–33. doi:10.1016/0022-2836(88)90132-5. PMID 2850369.
^ Weeds AG, Gooch J, Pope B, Harris HE (November 1986). "Preparation and characterization of pig plasma and platelet gelsolins". Eur. J. Biochem. 161 (1): 69–76. doi:10.1111/j.1432-1033.1986.tb10125.x. PMID 3023087.
^ Chauhan VP, Ray I, Chauhan A, Wisniewski HM (May 1999). "Binding of gelsolin, a secretory protein, to amyloid beta-protein". Biochem. Biophys. Res. Commun. 258 (2): 241–6. doi:10.1006/bbrc.1999.0623. PMID 10329371.
^ Nishimura K, Ting HJ, Harada Y, Tokizane T, Nonomura N, Kang HY, Chang HC, Yeh S, Miyamoto H, Shin M, Aozasa K, Okuyama A, Chang C (August 2003). "Modulation of androgen receptor transactivation by gelsolin: a newly identified androgen receptor coregulator". Cancer Res. 63 (16): 4888–94. PMID 12941811.
^ Wang Q, Xie Y, Du QS, Wu XJ, Feng X, Mei L, McDonald JM, Xiong WC (February 2003). "Regulation of the formation of osteoclastic actin rings by proline-rich tyrosine kinase 2 interacting with gelsolin". J. Cell Biol. 160 (4): 565–75. doi:10.1083/jcb.200207036. PMC 2173747. PMID 12578912.

External links

Gelsolin at the US National Library of Medicine Medical Subject Headings (MeSH)

http://www.bioaegistherapeutics.com

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. アミロイド疾患の遺伝的要因 genetic factors in the amyloid diseases
2. COPD治療における粘膜作用剤の役割 role of mucoactive agents in the treatment of copd
3. 腎アミロイドーシス renal amyloidosis
4. 全身性疾患のミオパシー myopathies of systemic disease
5. ポリオ後症候群 post polio syndrome

English Journal

Gelsolin (GSN) induces cardiomyocyte hypertrophy and BNP expression via p38 signaling and GATA-4 transcriptional factor activation.

Hu WS1, Ho TJ, Pai P, Chung LC, Kuo CH, Chang SH, Tsai FJ, Tsai CH, Jie YC, Liou YM, Huang CY.Author information 1PhD Program for Aging, China Medical University, Taichung, Taiwan, ROC.AbstractCardiomyocyte hypertrophy is an adaptive response of the heart to various types of stress. During the period of stress accumulation, the transition from physiological hypertrophy to pathological hypertrophy results in the promotion of heart failure. Gelsolin (GSN) is a member of the actin-binding proteins, which regulate dynamic actin filament organization by severing and capping. Moreover, GSN also regulates cell morphology, differentiation, movement, and apoptosis. In this study, we used H9c2 and H9c2-GSN stable clones in an attempt to understand the mechanisms of GSN overexpression in cardiomyocytes. These data showed that the overexpression of GSN in H9c2-induced cardiac hypertrophy and increased the pathological hypertrophy markers atrial natriuretic peptide brain natriuretic peptide. Furthermore, we found that E-cadherin expression decreased with the overexpression of GSN in H9c2, but β-catenin expression increased. These data presume that the cytoskeleton is loose. Further, previous studies show that the mitogen-activated protein kinase pathway can induce cardiac hypertrophy. Our data showed that p-p38 expression increased with the overexpression of GSN in H9c2, and the transcription factor p-GATA4 expression also increased, suggesting that the overexpression of GSN in H9c2-induced cardiac hypertrophy seemed to be regulated by the p38/GATA4 pathway. Moreover, we used both the p38 inhibitor (SB203580) and GSN siRNA to confirm our conjecture. We found that both of these factors significantly suppressed gelsolin-induced cardiac hypertrophy through p38/GATA4 signaling pathway. Therefore, we predict that the gene silencing of GSN and/or the downstream blocking of GSN along the p38 pathway could be applied to ameliorate pathological cardiac hypertrophy in the future.
Molecular and cellular biochemistry.Mol Cell Biochem.2014 May;390(1-2):263-70. doi: 10.1007/s11010-014-1977-7. Epub 2014 Feb 7.
Cardiomyocyte hypertrophy is an adaptive response of the heart to various types of stress. During the period of stress accumulation, the transition from physiological hypertrophy to pathological hypertrophy results in the promotion of heart failure. Gelsolin (GSN) is a member of the actin-binding pr
PMID 24505034

Proteomic study reveals plasma protein changes in congenital heart diseases.

Xuan C1, Gao G2, Yang Q3, Wang XL2, Liu ZG2, Liu XC2, He GW4.Author information 1TEDA International Cardiovascular Hospital, Tianjin and The Affiliated Hospital of Hangzhou Normal University, Hangzhou, China.2TEDA International Cardiovascular Hospital, Tianjin, China.3TEDA International Cardiovascular Hospital, Tianjin and The Affiliated Hospital of Hangzhou Normal University, Hangzhou, China; Department of Medicine and Therapeutics, The Chinese University of Hong Kong, Hong Kong, China.4TEDA International Cardiovascular Hospital, Tianjin and The Affiliated Hospital of Hangzhou Normal University, Hangzhou, China; Department of Surgery, Oregon Health and Science University, Portland, Oregon. Electronic address: gwhezj@163.com.AbstractBACKGROUND: Congenital heart disease (CHD) is the most common birth defect in newborns. Plasma proteins may serve as indicators of disease and are a rich source for biomarker discovery, but little has been studied in CHD. We examined the hypothesis that plasma proteins may be altered and related to the pathologic changes of CHD.
The Annals of thoracic surgery.Ann Thorac Surg.2014 Apr;97(4):1414-9. doi: 10.1016/j.athoracsur.2013.11.069. Epub 2014 Feb 22.
BACKGROUND: Congenital heart disease (CHD) is the most common birth defect in newborns. Plasma proteins may serve as indicators of disease and are a rich source for biomarker discovery, but little has been studied in CHD. We examined the hypothesis that plasma proteins may be altered and related to
PMID 24565402

The association between plasma gelsolin level and prognosis of burn patients.

Xianhui L1, Pinglian L2, Xiaojuan W1, Wei C1, Yong Y1, Feng R1, Peng S1, Gang X3.Author information 1Department of Burns and Plastic Surgery, Chengdu Military General Hospital, China.2Ganbu Ward, Chengdu Military General Hospital, China.3Department of Burns and Plastic Surgery, Chengdu Military General Hospital, China. Electronic address: tommy517@126.com.AbstractOBJECTIVE: To observe the change in plasma gelsolin levels among burn patients, and explore its impact on patient prognosis.
Burns : journal of the International Society for Burn Injuries.Burns.2014 Mar 29. pii: S0305-4179(14)00080-1. doi: 10.1016/j.burns.2014.02.020. [Epub ahead of print]
OBJECTIVE: To observe the change in plasma gelsolin levels among burn patients, and explore its impact on patient prognosis.METHODS: This prospective cohort study includes 98 burn patients with burns ≥30% TBSA, who were admitted to our institution between January 2010 and June 2013. Patients were
PMID 24690274

Japanese Journal

2P025 Single molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin(01B. Protein: Structure & Function,Poster)

Cao Yi,Lv Chunmei,Li Wenfei,Gao Xiang,Robinson Robert,Qin Meng,Burtnick Leslie,Wang Wei
生物物理 53(SUPPLEMENT_1-2), S163, 2013-09-13
NAID 110009819514

Mechanism of the Tissue-Specific Action of the Selective Androgen Receptor Modulator S-101479

Furuya Kazuyuki,Yamamoto Noriko,Ohyabu Yuki [他],Morikyu Teruyuki,Ishige Hirohide,Albers Michael,Endo Yasuhisa
Biological and Pharmaceutical Bulletin 36(3), 442-451, 2013
… Yeast two-hybrid interaction assays revealed that DHT promoted recruitment of numerous cofactors to AR such as TIF2, SRC1, β-catenin, NCoA3, gelsolin and PROX1 in a dose-dependent manner. … in particular, S-101479 failed to induce recruitment of canonical p160 coactivators such as SRC1, TIF2 and notably NCoA3 but only stimulated binding of AR to gelsolin and PROX1. …
NAID 130003382083

Overexpression of Gelsolin-Like Actin-Capping Protein Is Associated with Progression of Lung Adenocarcinoma

SHAO Fangchun,ZHANG Ruifeng,DONG Liangliang,YING Kejing
Tohoku journal of experimental medicine 225(2), 95-101, 2011-10-01
NAID 10029665821

Related Pictures

★リンクテーブル★

リンク元

「ゲルゾリン」

Gelsolin
	PDB rendering based on 1c0f.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1C0F, 1C0G, 1D4X, 1DEJ, 1EQY, 1ESV, 1H1V, 1KCQ, 1MDU, 1NLV, 1NM1, 1NMD, 1P8X, 1P8Z, 1SOL, 1T44, 1YAG, 1YVN, 2FF3, 2FF6, 2FH1, 2FH2, 2FH3, 2FH4, 3A5L, 3A5M, 3A5N, 3A5O, 3CI5, 3CIP, 3CJB, 3CJC, 3FFK, 3FFN, 3TU5, 4PKG, 4PKH, 4PKI
Identifiers
Symbols	GSN ; ADF; AGEL
External IDs	OMIM: 137350 MGI: 95851 HomoloGene: 147 GeneCards: GSN Gene
Gene ontology
Molecular function	• actin binding; • calcium ion binding; • protein binding; • protein domain specific binding; • myosin II binding;
Cellular component	• ruffle; • podosome; • extracellular region; • extracellular space; • nucleus; • cytoplasm; • cytosol; • plasma membrane; • focal adhesion; • actin cytoskeleton; • sarcoplasm; • lamellipodium; • actin cap; • cortical actin cytoskeleton; • myelin sheath; • perinuclear region of cytoplasm; • extracellular exosome; • blood microparticle;
Biological process	• phagocytosis, engulfment; • apoptotic process; • cellular component disassembly involved in execution phase of apoptosis; • aging; • positive regulation of gene expression; • programmed cell death; • oligodendrocyte development; • striated muscle atrophy; • extracellular matrix disassembly; • actin filament polymerization; • protein destabilization; • tissue regeneration; • sequestering of actin monomers; • actin nucleation; • response to ethanol; • negative regulation of viral entry into host cell; • phosphatidylinositol-mediated signaling; • actin filament severing; • barbed-end actin filament capping; • positive regulation of actin nucleation; • response to folic acid; • actin filament capping; • cilium morphogenesis; • cellular response to cadmium ion; • regulation of podosome assembly; • actin filament reorganization; • renal protein absorption; • hepatocyte apoptotic process; • positive regulation of keratinocyte apoptotic process; • regulation of wound healing, spreading of epidermal cells; • regulation of establishment of T cell polarity; • regulation of plasma membrane raft polarization; • regulation of receptor clustering; • positive regulation of protein processing in phagocytic vesicle; • amyloid fibril formation; • positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	v; t; e;

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Gelsolin
	crystal structure of the copii coat subunit, sec24, complexed with a peptide from the snare protein sed5 (yeast syntaxin-5)
Identifiers
Symbol	Gelsolin
Pfam	PF00626
Pfam clan	CL0092
InterPro	IPR007123
SCOP	1vil
SUPERFAMILY	1vil
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

　　[★]

英: gelsolin
関: ゲルソリン

[pmid24155256-1] Ghoshdastider U, Popp D, Burtnick LD, Robinson RC (2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton (Hoboken) 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256.

[Sun-2] Sun HQ, Yamamoto M, Mejillano M, Yin HL (November 1999). "Gelsolin, a multifunctional actin regulatory protein". J. Biol. Chem. 274 (47): 33179–82. doi:10.1074/jbc.274.47.33179. PMID 10559185.

[Koya-3] Koya RC, Fujita H, Shimizu S, Ohtsu M, Takimoto M, Tsujimoto Y, Kuzumaki N (May 2000). "Gelsolin inhibits apoptosis by blocking mitochondrial membrane potential loss and cytochrome c release". J. Biol. Chem. 275 (20): 15343–9. doi:10.1074/jbc.275.20.15343. PMID 10809769.

[Kiselar-4] Kiselar JG, Janmey PA, Almo SC, Chance MR (April 2003). "Visualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprinting". Proc. Natl. Acad. Sci. U.S.A. 100 (7): 3942–7. doi:10.1073/pnas.0736004100. PMC 153027. PMID 12655044.

[Yu-5] Yu FX, Sun HQ, Janmey PA, Yin HL (July 1992). "Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin". J. Biol. Chem. 267 (21): 14616–21. PMID 1321812.

[Burtnik-6] Burtnick LD, Urosev D, Irobi E, Narayan K, Robinson RC (July 2004). "Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF". EMBO J. 23 (14): 2713–22. doi:10.1038/sj.emboj.7600280. PMC 514944. PMID 15215896.

[Varon-7] Varon C, Tatin F, Moreau V, Van Obberghen-Schilling E, Fernandez-Sauze S, Reuzeau E, Kramer I, Génot E (May 2006). "Transforming growth factor beta induces rosettes of podosomes in primary aortic endothelial cells". Mol. Cell. Biol. 26 (9): 3582–94. doi:10.1128/MCB.26.9.3582-3594.2006. PMC 1447430. PMID 16611998.

[pmid11039896-8] Kusano H, Shimizu S, Koya RC, Fujita H, Kamada S, Kuzumaki N, Tsujimoto Y (October 2000). "Human gelsolin prevents apoptosis by inhibiting apoptotic mitochondrial changes via closing VDAC". Oncogene 19 (42): 4807–14. doi:10.1038/sj.onc.1203868. PMID 11039896.

[Witke-9] Witke W, Sharpe AH, Hartwig JH, Azuma T, Stossel TP, Kwiatkowski DJ (April 1995). "Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin". Cell 81 (1): 41–51. doi:10.1016/0092-8674(95)90369-0. PMID 7720072.

[Becker-10] Becker PM, Kazi AA, Wadgaonkar R, Pearse DB, Kwiatkowski D, Garcia JG (April 2003). "Pulmonary vascular permeability and ischemic injury in gelsolin-deficient mice". Am. J. Respir. Cell Mol. Biol. 28 (4): 478–84. doi:10.1165/rcmb.2002-0024OC. PMID 12654637.

[pmid2850369-11] Way M, Weeds A (October 1988). "Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats". J. Mol. Biol. 203 (4): 1127–33. doi:10.1016/0022-2836(88)90132-5. PMID 2850369.

[pmid3023087-12] Weeds AG, Gooch J, Pope B, Harris HE (November 1986). "Preparation and characterization of pig plasma and platelet gelsolins". Eur. J. Biochem. 161 (1): 69–76. doi:10.1111/j.1432-1033.1986.tb10125.x. PMID 3023087.

[pmid10329371-13] Chauhan VP, Ray I, Chauhan A, Wisniewski HM (May 1999). "Binding of gelsolin, a secretory protein, to amyloid beta-protein". Biochem. Biophys. Res. Commun. 258 (2): 241–6. doi:10.1006/bbrc.1999.0623. PMID 10329371.

[pmid12941811-14] Nishimura K, Ting HJ, Harada Y, Tokizane T, Nonomura N, Kang HY, Chang HC, Yeh S, Miyamoto H, Shin M, Aozasa K, Okuyama A, Chang C (August 2003). "Modulation of androgen receptor transactivation by gelsolin: a newly identified androgen receptor coregulator". Cancer Res. 63 (16): 4888–94. PMID 12941811.

[pmid12578912-15] Wang Q, Xie Y, Du QS, Wu XJ, Feng X, Mei L, McDonald JM, Xiong WC (February 2003). "Regulation of the formation of osteoclastic actin rings by proline-rich tyrosine kinase 2 interacting with gelsolin". J. Cell Biol. 160 (4): 565–75. doi:10.1083/jcb.200207036. PMC 2173747. PMID 12578912.

匿名

検索

案内

案内

gelsolin