Paxillin

PXN
Paxillin is a protein that in humans is encoded by the PXN gene.wikipedia
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Extracellular matrix

ECMmatrixextracellular matrices
Paxillin is expressed at focal adhesions of non-striated cells and at costameres of striated muscle cells, and it functions to adhere cells to the extracellular matrix.
This complex contains many proteins that are essential to durotaxis including structural anchoring proteins (integrins) and signaling proteins (adhesion kinase (FAK), talin, vinculin, paxillin, α-actinin, GTPases etc.) which cause changes in cell shape and actomyosin contractility.

Keith Burridge

Paxillin is a signal transduction adaptor protein discovered in 1990 in the laboratory of Keith Burridge The C-terminal region of paxillin contains four LIM domains that target paxillin to focal adhesions.
His research on focal adhesions includes the discovery of many adhesion proteins including vinculin, talin and paxillin, and ranks him in top 1% of the most cited scientist in the field of molecular biology and genetics.

PTK2

focal adhesion kinaseFAKfocal adhesion kinase (FAK)
The N-terminal region of paxillin has five highly conserved leucine-rich sequences termed LD motifs, which mediate several interactions, including that with pp125FAK and vinculin. The proteins that bind to paxillin are diverse and include protein tyrosine kinases, such as Src and focal adhesion kinase (FAK), structural proteins, such as vinculin and actopaxin, and regulators of actin organization, such as COOL/PIX and PKL/GIT.
Additional components of focal adhesions include actin, filamin, vinculin, talin, paxillin, tensin and RSU-1.

Focal adhesion

focal adhesionsadhesion plaquesfocal-adhesion
Paxillin is expressed at focal adhesions of non-striated cells and at costameres of striated muscle cells, and it functions to adhere cells to the extracellular matrix. Paxillin is a signal transduction adaptor protein discovered in 1990 in the laboratory of Keith Burridge The C-terminal region of paxillin contains four LIM domains that target paxillin to focal adhesions. The C-terminal region of paxillin is composed of four tandem double zinc finger LIM domains that are cysteine/histidine-rich with conserved repeats; these serve as binding sites for the protein tyrosine phosphatase-PEST, tubulin and serves as the targeting motif for focal adhesions.
Initially, small (0.25μm²) focal adhesions called focal complexes (FXs) are formed at the leading edge of the cell in lamellipodia: they consist of integrin, and some of the adapter proteins, such as talin, paxillin and tensin.

PTPN12

PTP-PESTProtein tyrosine phosphatase, non-receptor type 12protein tyrosine phosphatase-PEST
The C-terminal region of paxillin is composed of four tandem double zinc finger LIM domains that are cysteine/histidine-rich with conserved repeats; these serve as binding sites for the protein tyrosine phosphatase-PEST, tubulin and serves as the targeting motif for focal adhesions.
PTPN12 has been shown to interact with BCAR1, Grb2, PSTPIP1, TGFB1I1, Paxillin and SHC1.

Integrin

integrinsintegrin receptorintegrin alpha1
It is presumed through a direct association with the cytoplasmic tail of beta-integrin.
The attachment of the cell takes place through formation of cell adhesion complexes, which consist of integrins and many cytoplasmic proteins, such as talin, vinculin, paxillin, and alpha-actinin.

Vinculin

VCLMetavinculin
The N-terminal region of paxillin has five highly conserved leucine-rich sequences termed LD motifs, which mediate several interactions, including that with pp125FAK and vinculin. The proteins that bind to paxillin are diverse and include protein tyrosine kinases, such as Src and focal adhesion kinase (FAK), structural proteins, such as vinculin and actopaxin, and regulators of actin organization, such as COOL/PIX and PKL/GIT.

CRKL

Crk-LCRKL-C3Gv-Crk SH2
Three N-terminal YXXP motifs may serve as binding sites for talin or v-Crk SH2.

Proto-oncogene tyrosine-protein kinase Src

Srcc-Srcv-src
The proteins that bind to paxillin are diverse and include protein tyrosine kinases, such as Src and focal adhesion kinase (FAK), structural proteins, such as vinculin and actopaxin, and regulators of actin organization, such as COOL/PIX and PKL/GIT.

Adapter molecule crk

CRKv-CrkCRK (gene)
Paxillin is tyrosine-phosphorylated by FAK and Src upon integrin engagement or growth factor stimulation, creating binding sites for the adapter protein Crk.

SORBS1

CAP/ponsinponsin
The proline-rich region of paxillin specifically binds to the second SH3 domain of ponsin, which occurs after the onset of the myogenic differentiation and with expression restricted to costameres.

Protein

proteinsproteinaceousstructural proteins
Paxillin is a protein that in humans is encoded by the PXN gene.

Gene

genesnumber of genesgene sequence
Paxillin is a protein that in humans is encoded by the PXN gene.

Costamere

dystrophin-glycoprotein complexDPCdystrophin-associated glycoprotein complex
Paxillin is expressed at focal adhesions of non-striated cells and at costameres of striated muscle cells, and it functions to adhere cells to the extracellular matrix. The proline-rich region of paxillin specifically binds to the second SH3 domain of ponsin, which occurs after the onset of the myogenic differentiation and with expression restricted to costameres.

Striated muscle tissue

striated musclestriationsstriated
Paxillin is expressed at focal adhesions of non-striated cells and at costameres of striated muscle cells, and it functions to adhere cells to the extracellular matrix.

Amino acid

amino acidsresiduesresidue
Human paxillin is 64.5 kDa in molecular weight and 591 amino acids in length.

C-terminus

C-terminalC-terminal domainC terminus
The C-terminal region of paxillin is composed of four tandem double zinc finger LIM domains that are cysteine/histidine-rich with conserved repeats; these serve as binding sites for the protein tyrosine phosphatase-PEST, tubulin and serves as the targeting motif for focal adhesions.

Zinc finger

zinc-fingerzinc finger proteinzinc fingers
The C-terminal region of paxillin is composed of four tandem double zinc finger LIM domains that are cysteine/histidine-rich with conserved repeats; these serve as binding sites for the protein tyrosine phosphatase-PEST, tubulin and serves as the targeting motif for focal adhesions.

LIM domain

LIMLIM homeobox
Paxillin is a signal transduction adaptor protein discovered in 1990 in the laboratory of Keith Burridge The C-terminal region of paxillin contains four LIM domains that target paxillin to focal adhesions. The C-terminal region of paxillin is composed of four tandem double zinc finger LIM domains that are cysteine/histidine-rich with conserved repeats; these serve as binding sites for the protein tyrosine phosphatase-PEST, tubulin and serves as the targeting motif for focal adhesions.

Cysteine

CysL-cysteinecystein
The C-terminal region of paxillin is composed of four tandem double zinc finger LIM domains that are cysteine/histidine-rich with conserved repeats; these serve as binding sites for the protein tyrosine phosphatase-PEST, tubulin and serves as the targeting motif for focal adhesions.

Histidine

Hishistidine metabolismhistidines
The C-terminal region of paxillin is composed of four tandem double zinc finger LIM domains that are cysteine/histidine-rich with conserved repeats; these serve as binding sites for the protein tyrosine phosphatase-PEST, tubulin and serves as the targeting motif for focal adhesions.

Tubulin

β-tubulinγ-tubulinα-tubulin
The C-terminal region of paxillin is composed of four tandem double zinc finger LIM domains that are cysteine/histidine-rich with conserved repeats; these serve as binding sites for the protein tyrosine phosphatase-PEST, tubulin and serves as the targeting motif for focal adhesions.

N-terminus

N-terminalN terminusN-
The N-terminal region of paxillin has five highly conserved leucine-rich sequences termed LD motifs, which mediate several interactions, including that with pp125FAK and vinculin. Three N-terminal YXXP motifs may serve as binding sites for talin or v-Crk SH2.

Leucine

LeuL-leucineL
The N-terminal region of paxillin has five highly conserved leucine-rich sequences termed LD motifs, which mediate several interactions, including that with pp125FAK and vinculin. The LD motifs are predicted to form amphipathic alpha helices, with each leucine residue positioned on one face of the alpha helix to form a hydrophobic protein-binding interface.

Alpha helix

alpha helicesα-helicesalpha-helices
The LD motifs are predicted to form amphipathic alpha helices, with each leucine residue positioned on one face of the alpha helix to form a hydrophobic protein-binding interface.