Colleagues, friends, and family of Lester “Skip” Binder are mourning his sudden passing on November 15, a month shy of his 64th birthday.

Known to his fellow researchers as “The Godfather of Tau,” Binder was among the first to recognize that the protein makes up the bulk of neurofibrillary tangles (see Wood et al., 1986). He laid much of the groundwork supporting the idea that tau contributes to neurodegeneration. Formerly a professor at Northwestern University in Chicago, Binder had recently taken up a position at Michigan State University in Grand Rapids, Michigan.

In addition to his scientific prowess, collaborators remember him for his outgoing personality, wit, and generous nature. “He was a font of ideas that we will all miss, and had an irrepressible humor that partnered perfectly with his science,” Kenneth Kosik, University of California, Santa Barbara, wrote to Alzforum in an email (see full tribute below).

 

image

Lester "Skip" Binder. Image courtesy of the Binder family.

Binder earned a Ph.D. from Yale University in 1978, and it was there that he began studying microtubules. Throughout his career, he explored the molecular machinations that lead to tangles (see April 2006 news story). “He really started the field of tau,” said Elliott Mufson, Rush University, Chicago. “Up until the day that he died, he was at the forefront of its involvement in AD.” Mufson remarked on the high quality of Binder’s papers, one of which earned him the 2004 Alzheimer Award from the Journal of Alzheimer’s Disease.

“Skip didn’t care about flash and wasn’t interested in awards,” Mufson told Alzforum, saying that Binder focused on generating new discoveries at the bench and collaborating with fellow scientists. Binder made some of the first antibodies to tau, including tau-1 (see Binder et al., 1985; Ksiezak-Reding et al., 1988), and generated a large number of them over his career, most recently against tau oligomers (see Patterson et al., 2011; Ward et al., 2013). In keeping with his collegial nature, Binder shared these antibodies widely.

Binder actively mentored his students, said his colleage Sandra Weintraub, Northwestern University. She added that his zest for life made him a magnetic personality. “When he came into a room, it was like, ‘The party starts now,’” she remembered. In addition to a passion for science, Binder loved his family and was a connoisseur of fine food and wine. “He knew wine like he knew tau,” joked Mufson.

Binder died suddenly, from a longstanding heart condition, in the place he loved best: the great outdoors during an annual hunting trip with his brother at the family’s farm in Caro, Michigan. For more details about Binder's life, see his obituary.

Alzforum invites all who knew Binder to pay tribute or share a memory.—Gwyneth Dickey Zakaib

Comments

  1. Irreverent, witty, lively, and always full of kindness and generosity, Skip’s untimely death must give pause to all of us who knew him, and many more who only knew of him. We should build upon his insights as we delve ever more deeply into the diseases that today we call the tauopathies. Lester Binder, known to his friends as Skip, was trained as a cell biologist and it was in that setting—the American Society for Cell Biology meeting—where I met him. That was before we knew that tau protein formed the classical Alzheimer’s disease hallmark, the neurofibrillary tangle. He stopped at my poster and told me more about my own data than I even remotely suspected was apparent in those gels of microtubule fractions. That moment triggered a long-term shared interest in microtubule-associated proteins, and when our labs independently found tau immunoreactivity in neurofibrillary tangles, we exchanged our data prepublication and copublished. The importance Skip placed on collegiality and inclusiveness stand as much to his legacy as the foundational findings that came from his lab. He was an early adopter of the monoclonal antibody technique first described in 1975 by Georges J.F. Köhler and César Milstein. Using this approach, Skip had an almost magical ability to generate novel monoclonal antibodies to tau and he certainly stands as a forbear to the intense interest today in tau antibodies as a possible therapeutics. Over many years at Northwestern University, Skip was adored by the many students he trained, and he was cherished by colleagues. He enjoyed the people who do the science as much as the science itself. He was a font of ideas whom we will all miss, and he had an irrepressible humor that partnered perfectly with his science. In the words of Arthur Rimbaud’s “Farewell”: “Autumn already!—But why regret an eternal sun if we are embarked on the discovery of divine light—far from all those who fret over seasons.”

  2. I was a postdoc in Skip’s lab at Northwestern from 1998-2002 and we were good friends and colleagues after that. Skip was incredibly generous with his time and friendship. He was always there for people, no matter what. His passing makes one realize just how much he meant to me personally and to the field. Skip's was among the groups that first identified tau as the major component of neurofibrillary tangles, and he was at the forefront of the struggle to get the field to recognize tau as a major contributor to the neurodegenerative process rather than a byproduct. The antibodies he developed helped move the field forward tremendously, and his work into the mechanisms that cause tau to misfold and aggregate were groundbreaking.

    It still doesn’t seem real that he is gone. Skip was a lot of things to a lot of people—an extraordinary researcher, a mentor, a colleague, a friend, a loving husband, a devoted father—and he was one of the best at all those things. I will miss him very much.

  3. Very simply, Skip was a wonderful person, mentor, scientist, and friend. His generosity seemed to know no bounds, and his exceptional intelligence and rigorous research earned him respect and admiration from his colleagues and friends across the globe. He found great joy and pride in the success of others around him and those of us who were lucky enough to be part of his research family. Skip was best known for his numerous and significant contributions to the tau field. He is world-renowned for making antibodies against tau, many of which have provided invaluable insight into the pathobiology of tau in diseases such as Alzheimer's disease and tauopathies. Skip often liked to remind us of Bertrand Russell’s words that science aims “to approach the truth by successive approximations.” Our ability to approximate the truth has taken a hit with the loss of such a great man.

  4. We will miss his generosity in sharing information and antibodies, his stuborness and his willingness to discuss, his big mind in his big body ...

Make a Comment

To make a comment you must login or register.

References

News Citations

  1. Keystone Symposia Meeting, Part 6—Tau and FTD

Paper Citations

  1. . Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau). Proc Natl Acad Sci U S A. 1986 Jun;83(11):4040-3. PubMed.
  2. . The distribution of tau in the mammalian central nervous system. J Cell Biol. 1985 Oct;101(4):1371-8. PubMed.
  3. . Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1. J Biol Chem. 1988 Jun 15;263(17):7948-53. PubMed.
  4. . Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease. J Biol Chem. 2011 Jul 1;286(26):23063-76. PubMed.
  5. . TOC1: Characterization of a Selective Oligomeric Tau Antibody. J Alzheimers Dis. 2013;37(3):593-602. PubMed.

External Citations

  1. 2004 Alzheimer Award
  2. obituary

Further Reading

Papers

  1. . Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1. J Biol Chem. 1988 Jun 15;263(17):7948-53. PubMed.
  2. . TOC1: Characterization of a Selective Oligomeric Tau Antibody. J Alzheimers Dis. 2013;37(3):593-602. PubMed.
  3. . Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease. J Biol Chem. 2011 Jul 1;286(26):23063-76. PubMed.