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Gene Review

PAN1  -  Pan1p

Saccharomyces cerevisiae S288c

Synonyms: Actin cytoskeleton-regulatory complex protein PAN1, DIM2, MDP3, MIP3, Mitochondrial distribution of proteins protein 3, ...
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High impact information on PAN1

  • We suggest that Pan1p forms the core of an endocytic complex and physically couples actin polymerization nucleated by the Arp2/3 complex to the endocytic machinery, thus providing the forces necessary for endocytosis [1].
  • Here we show that the yeast endocytic protein Pan1p binds to and activates the Arp2/3 complex [1].
  • In vitro phosphorylation assays demonstrate that Prk1p is able to phosphorylate regions of Pan1p containing the LxxQxTG repeats, including the region responsible for binding to End3p [2].
  • Normal actin cytoskeleton organization in budding yeast requires the function of the Pan1p/ End3p complex [2].
  • By screening for mutations that can suppress the temperature sensitivity of a pan1 mutant (pan1-4), a novel serine/threonine kinase Prk1p is now identified as a new factor regulating the actin cytoskeleton organization in yeast [2].

Biological context of PAN1


Anatomical context of PAN1

  • Phosphorylated Pan1p is probably then dephosphorylated in the cytosol [7].
  • Pan1p is a homologue of the mammalian protein eps15, which has been implicated in endocytosis by virtue of its association with the plasma membrane clathrin adaptor complex AP-2 [4].
  • These cell wall defects are also exhibited by wild-type cells overproducing the C-terminal region of Sla1p that is responsible for interactions with Pan1p and End3p [5].

Associations of PAN1 with chemical compounds

  • We observed genetic interactions between the yeast SJL1 gene and PAN1, which suggest a role for phosphoinositide metabolites in Pan1p function [4].
  • Pan1p, an actin cytoskeleton-associated protein, is required for growth of yeast on oleate medium [8].
  • Pan1p, which binds several other endocytic proteins, is composed of multiple protein-protein interaction domains including two Eps15 Homology (EH) domains, a coiled-coil domain, an acidic Arp2/3-activating region, and a proline-rich domain [6].

Co-localisations of PAN1


Regulatory relationships of PAN1

  • Synthetic growth defects were observed in a pan1-20 ENT1(EE) double mutant, suggesting that Ent1p phosphorylation negatively regulates the formation/activity of a Pan1p-Ent1p complex [10].
  • Overall, our results establish that Sla2p's regulation of Pan1p plays an important role in controlling Pan1p-stimulated actin polymerization during endocytosis [7].
  • Pan1p activity is negatively regulated by Prk1 kinase phosphorylation after endocytic internalization [7].
  • Interestingly, Sla2p specifically inhibited Pan1p Arp2/3 complex activation activity in vitro [7].

Other interactions of PAN1

  • The suppression of pan1-4 by prk1 requires the presence of mutant Pan1p [2].
  • MDP3 is identical to PAN1, which encodes a protein involved in initiation of translation and actin cytoskeleton organization [11].
  • Yeast Eps15-like endocytic protein, Pan1p, activates the Arp2/3 complex [1].
  • This new screening strategy demonstrates a role for She4p and Pan1p in endocytosis, and provides a new general method for the identification of additional endocytosis mutants [12].
  • These data confirm that Pan2p and not Pan1p is required for PAN activity, and they suggest that ribonucleases other than the Pab1p-stimulated PAN are capable of shortening poly(A) tails in vivo [13].

Analytical, diagnostic and therapeutic context of PAN1


  1. Yeast Eps15-like endocytic protein, Pan1p, activates the Arp2/3 complex. Duncan, M.C., Cope, M.J., Goode, B.L., Wendland, B., Drubin, D.G. Nat. Cell Biol. (2001) [Pubmed]
  2. Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p. Zeng, G., Cai, M. J. Cell Biol. (1999) [Pubmed]
  3. The EH-domain-containing protein Pan1 is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae. Tang, H.Y., Cai, M. Mol. Cell. Biol. (1996) [Pubmed]
  4. Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis. Wendland, B., Emr, S.D. J. Cell Biol. (1998) [Pubmed]
  5. Pan1p, End3p, and S1a1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis. Tang, H.Y., Xu, J., Cai, M. Mol. Cell. Biol. (2000) [Pubmed]
  6. The function of the endocytic scaffold protein Pan1p depends on multiple domains. Miliaras, N.B., Park, J.H., Wendland, B. Traffic (2004) [Pubmed]
  7. Negative Regulation of Yeast Eps15-like Arp2/3 Complex Activator, Pan1p, by the Hip1R-related Protein, Sla2p, during Endocytosis. Toshima, J., Toshima, J.Y., Duncan, M.C., Cope, M.J., Sun, Y., Martin, A.C., Anderson, S., Yates, J.R., Mizuno, K., Drubin, D.G. Mol. Biol. Cell (2007) [Pubmed]
  8. Pan1p, an actin cytoskeleton-associated protein, is required for growth of yeast on oleate medium. Kamińska, J., Wysocka-Kapcińska, M., Smaczyńska-de Rooij, I., Rytka, J., Zoładek, T. Exp. Cell Res. (2005) [Pubmed]
  9. Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae. Kamińska, J., Gajewska, B., Hopper, A.K., Zoładek, T. Mol. Cell. Biol. (2002) [Pubmed]
  10. In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation. Watson, H.A., Cope, M.J., Groen, A.C., Drubin, D.G., Wendland, B. Mol. Biol. Cell (2001) [Pubmed]
  11. MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5. Zoladek, T., Tobiasz, A., Vaduva, G., Boguta, M., Martin, N.C., Hopper, A.K. Genetics (1997) [Pubmed]
  12. A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15. Wendland, B., McCaffery, J.M., Xiao, Q., Emr, S.D. J. Cell Biol. (1996) [Pubmed]
  13. The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity. Boeck, R., Tarun, S., Rieger, M., Deardorff, J.A., Müller-Auer, S., Sachs, A.B. J. Biol. Chem. (1996) [Pubmed]
  14. Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX. Voss, H., Tamames, J., Teodoru, C., Valencia, A., Sensen, C., Wiemann, S., Schwager, C., Zimmermann, J., Sander, C., Ansorge, W. Yeast (1995) [Pubmed]
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